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Conserved domains on  [gi|2507698970|ref|XP_056078905|]
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uncharacterized protein SMKI_13G4370 [Saccharomyces mikatae IFO 1815]

Protein Classification

NAD(P)-dependent alcohol dehydrogenase( domain architecture ID 10143012)

NAD(P)-dependent alcohol dehydrogenase catalyzes the reversible conversion of an alcohol to its corresponding aldehyde

CATH:  3.40.50.720|3.90.180.10
EC:  1.1.-.-
Gene Ontology:  GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-351 1.65e-154

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


:

Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 437.70  E-value: 1.65e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970   8 EGIAIQSHEdwKNPKKTKYDPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKV 87
Cdd:cd05283     1 KGYAARDAS--GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKV-TKFKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  88 GQRVGVGAQVFSCLECDRCKSDNEPYCTKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT 167
Cdd:cd05283    78 GDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGIT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 168 VYSPLVRNGCGPGKKvgivglggigsMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWgEKYFDTFDLI 247
Cdd:cd05283   158 VYSPLKRNGVGPGKRvgvvgigglghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAM-KKAAGSLDLI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 248 VVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHemLTLKPYGL--KAVSISYSALGSIKELKQLLALVSEKNIKVWVET 325
Cdd:cd05283   237 IDTVSA--SHDLDPYLSLLKPGGTLVLVGAPEEP--LPVPPFPLifGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEV 312

                         330       340
                  ....*....|....*....|....*.
gi 2507698970 326 LPVgeAGVHEALERMERGDVRYRFTL 351
Cdd:cd05283   313 IPM--DGINEALERLEKGDVRYRFVL 336
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-351 1.65e-154

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 437.70  E-value: 1.65e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970   8 EGIAIQSHEdwKNPKKTKYDPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKV 87
Cdd:cd05283     1 KGYAARDAS--GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKV-TKFKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  88 GQRVGVGAQVFSCLECDRCKSDNEPYCTKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT 167
Cdd:cd05283    78 GDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGIT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 168 VYSPLVRNGCGPGKKvgivglggigsMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWgEKYFDTFDLI 247
Cdd:cd05283   158 VYSPLKRNGVGPGKRvgvvgigglghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAM-KKAAGSLDLI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 248 VVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHemLTLKPYGL--KAVSISYSALGSIKELKQLLALVSEKNIKVWVET 325
Cdd:cd05283   237 IDTVSA--SHDLDPYLSLLKPGGTLVLVGAPEEP--LPVPPFPLifGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEV 312

                         330       340
                  ....*....|....*....|....*.
gi 2507698970 326 LPVgeAGVHEALERMERGDVRYRFTL 351
Cdd:cd05283   313 IPM--DGINEALERLEKGDVRYRFVL 336
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 27-351 6.65e-98

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 293.56  E-value: 6.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAqVFSCLECDRC 106
Cdd:COG1064    22 EPGP---GEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGV-TGFKVGDRVGVGW-VDSCGTCEYC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKvgiv 186
Cdd:COG1064    97 RSGRENLCENGRFT-------GYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAGVGPGDRvavi 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 glggigSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATlEEGDWGEKYFD--TFDLIVVCASSltDIDFNIMPK 264
Cdd:COG1064   170 gagglgHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNS-SDEDPVEAVREltGADVVIDTVGA--PATVNAALA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 265 AMKVGGRIVSISIPEqhEMLTLKPYGL--KAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEAGvhEALERMER 342
Cdd:COG1064   247 LLRRGGRLVLVGLPG--GPIPLPPFDLilKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIPLEEAN--EALERLRA 322


                  ....*....
gi 2507698970 343 GDVRYRFTL 351
Cdd:COG1064   323 GKVRGRAVL 331
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 35-351 3.26e-65

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 210.42  E-value: 3.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFSCLECDRCKSDNEPYC 114
Cdd:PLN02514   36 DVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDV-SKFTVGDIVGVGVIVGCCGECSPCKSDLEQYC 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 115 TKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVR-NGCGPGKKVGIVGLGGIGS 193
Cdd:PLN02514  115 NKRIWSYNDVYTDGKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHfGLKQSGLRGGILGLGGVGH 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 194 MGTLISKAMGAETYVISRSSKKKEDAIK-MGADHYIATLEEGDWgEKYFDTFDLIVVCASSLTDIDFNImpKAMKVGGRI 272
Cdd:PLN02514  195 MGVKIAKAMGHHVTVISSSDKKREEALEhLGADDYLVSSDAAEM-QEAADSLDYIIDTVPVFHPLEPYL--SLLKLDGKL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 273 V---SISIPEQ--HEMLTLkpyGLKAVSISYsaLGSIKELKQLLALVSEKNIKVWVETLPVGEagVHEALERMERGDVRY 347
Cdd:PLN02514  272 IlmgVINTPLQfvTPMLML---GRKVITGSF--IGSMKETEEMLEFCKEKGLTSMIEVVKMDY--VNTAFERLEKNDVRY 344


                  ....
gi 2507698970 348 RFTL 351
Cdd:PLN02514  345 RFVV 348
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 34-148 3.69e-35

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 124.26  E-value: 3.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVfSCLECDRCKSDNEPY 113
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGP-GVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2507698970 114 CTKFVTTysqpyedGYISQGGYANYVRVHEHFIVP 148
Cdd:pfam08240  79 CPNGRFL-------GYDRDGGFAEYVVVPERNLVP 106
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 38-224 7.32e-22

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 94.60  E-value: 7.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  38 IKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVGAQVFSCLECDRCKSDNEPYCTKf 117
Cdd:TIGR02822  32 VRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRG-ADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAENLCPA- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 118 vTTYSqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTL 197
Cdd:TIGR02822 110 -SRYT-----GWDTDGGYAEYTTVPAAFAYRLPTGYDDVELAPLLCAGIIGYRALLRASLPPGGRLGLYGFGGSAHLTAQ 183

                         170       180
                  ....*....|....*....|....*..
gi 2507698970 198 ISKAMGAETYVISRSSKKKEDAIKMGA 224
Cdd:TIGR02822 184 VALAQGATVHVMTRGAAARRLALALGA 210
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 38-343 3.16e-07

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 51.23  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970   38 IKIEACGVCGSDVHCAAGhwgNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVgVGaqvfsclecdrcksdnepyctkf 117
Cdd:smart00829   1 IEVRAAGLNFRDVLIALG---LYPGEAVLGGECAGVVTRVGP-GVTGLAVGDRV-MG----------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  118 vttysqpyedgyISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVY-------------SPLVRNGCGpgkkvg 184
Cdd:smart00829  53 ------------LAPGAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYyalvdlarlrpgeSVLIHAAAG------ 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  185 ivglggigsmGT-----LISKAMGAETYViSRSSKKKEDAIK-MG-ADHYI--------------ATLEEGdwgekyfdt 243
Cdd:smart00829 115 ----------GVgqaaiQLARHLGAEVFA-TAGSPEKRDFLRaLGiPDDHIfssrdlsfadeilrATGGRG--------- 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  244 FDLIVvcaSSLTDiDFniMPKAMKV---GGRIVSISI-----PEQHEMLTLKPyglkavSISYSA--LGSIKE------- 306
Cdd:smart00829 175 VDVVL---NSLSG-EF--LDASLRClapGGRFVEIGKrdirdNSQLAMAPFRP------NVSYHAvdLDALEEgpdrire 242

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2507698970  307 -LKQLLALVSEKNIK-VWVETLPVGEagVHEALERMERG 343
Cdd:smart00829 243 lLAEVLELFAEGVLRpLPVTVFPISD--AEDAFRYMQQG 279
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-351 1.65e-154

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 437.70  E-value: 1.65e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970   8 EGIAIQSHEdwKNPKKTKYDPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKV 87
Cdd:cd05283     1 KGYAARDAS--GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKV-TKFKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  88 GQRVGVGAQVFSCLECDRCKSDNEPYCTKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT 167
Cdd:cd05283    78 GDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGIT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 168 VYSPLVRNGCGPGKKvgivglggigsMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWgEKYFDTFDLI 247
Cdd:cd05283   158 VYSPLKRNGVGPGKRvgvvgigglghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAM-KKAAGSLDLI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 248 VVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHemLTLKPYGL--KAVSISYSALGSIKELKQLLALVSEKNIKVWVET 325
Cdd:cd05283   237 IDTVSA--SHDLDPYLSLLKPGGTLVLVGAPEEP--LPVPPFPLifGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEV 312

                         330       340
                  ....*....|....*....|....*.
gi 2507698970 326 LPVgeAGVHEALERMERGDVRYRFTL 351
Cdd:cd05283   313 IPM--DGINEALERLEKGDVRYRFVL 336
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 10-351 1.59e-150

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 427.12  E-value: 1.59e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  10 IAIQSHEDWKNPKKTKYDPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSNsGLKVGQ 89
Cdd:cd08245     1 KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVE-GRKVGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  90 RVGVGAQVFSCLECDRCKSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVY 169
Cdd:cd08245    80 RVGVGWLVGSCGRCEYCRRGLENLCQKAVNT-------GYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 170 SPLVRNGCGPGKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEkYFDTFDLIVV 249
Cdd:cd08245   153 SALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQA-AAGGADVILV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 250 CASSLTdiDFNIMPKAMKVGGRIVSISIPEQHEML-TLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPV 328
Cdd:cd08245   232 TVVSGA--AAEAALGGLRRGGRIVLVGLPESPPFSpDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETFPL 309

                         330       340
                  ....*....|....*....|...
gi 2507698970 329 geAGVHEALERMERGDVRYRFTL 351
Cdd:cd08245   310 --DQANEAYERMEKGDVRFRFVL 330
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 27-351 6.65e-98

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 293.56  E-value: 6.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAqVFSCLECDRC 106
Cdd:COG1064    22 EPGP---GEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGV-TGFKVGDRVGVGW-VDSCGTCEYC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKvgiv 186
Cdd:COG1064    97 RSGRENLCENGRFT-------GYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAGVGPGDRvavi 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 glggigSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATlEEGDWGEKYFD--TFDLIVVCASSltDIDFNIMPK 264
Cdd:COG1064   170 gagglgHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNS-SDEDPVEAVREltGADVVIDTVGA--PATVNAALA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 265 AMKVGGRIVSISIPEqhEMLTLKPYGL--KAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEAGvhEALERMER 342
Cdd:COG1064   247 LLRRGGRLVLVGLPG--GPIPLPPFDLilKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIPLEEAN--EALERLRA 322


                  ....*....
gi 2507698970 343 GDVRYRFTL 351
Cdd:COG1064   323 GKVRGRAVL 331
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 35-351 3.26e-65

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 210.42  E-value: 3.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFSCLECDRCKSDNEPYC 114
Cdd:PLN02514   36 DVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDV-SKFTVGDIVGVGVIVGCCGECSPCKSDLEQYC 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 115 TKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVR-NGCGPGKKVGIVGLGGIGS 193
Cdd:PLN02514  115 NKRIWSYNDVYTDGKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHfGLKQSGLRGGILGLGGVGH 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 194 MGTLISKAMGAETYVISRSSKKKEDAIK-MGADHYIATLEEGDWgEKYFDTFDLIVVCASSLTDIDFNImpKAMKVGGRI 272
Cdd:PLN02514  195 MGVKIAKAMGHHVTVISSSDKKREEALEhLGADDYLVSSDAAEM-QEAADSLDYIIDTVPVFHPLEPYL--SLLKLDGKL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 273 V---SISIPEQ--HEMLTLkpyGLKAVSISYsaLGSIKELKQLLALVSEKNIKVWVETLPVGEagVHEALERMERGDVRY 347
Cdd:PLN02514  272 IlmgVINTPLQfvTPMLML---GRKVITGSF--IGSMKETEEMLEFCKEKGLTSMIEVVKMDY--VNTAFERLEKNDVRY 344


                  ....
gi 2507698970 348 RFTL 351
Cdd:PLN02514  345 RFVV 348
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 33-351 1.07e-64

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 209.35  E-value: 1.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVGAQVFSCLECDRCKSDNEP 112
Cdd:PLN02586   37 DEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLG-KNVKKFKEGDRVGVGVIVGSCKSCESCDQDLEN 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 113 YCTKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNG-CGPGKKVGIVGLGGI 191
Cdd:PLN02586  116 YCPKMIFTYNSIGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGmTEPGKHLGVAGLGGL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 192 GSMGTLISKAMGAETYVISRSSKKKEDAI-KMGADHYIATLEEGDWgEKYFDTFDLIVVCASSLTDIdfNIMPKAMKVGG 270
Cdd:PLN02586  196 GHVAVKIGKAFGLKVTVISSSSNKEDEAInRLGADSFLVSTDPEKM-KAAIGTMDYIIDTVSAVHAL--GPLLGLLKVNG 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 271 RIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEagVHEALERMERGDVRYRFT 350
Cdd:PLN02586  273 KLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDE--INTAMERLAKSDVRYRFV 350


                  .
gi 2507698970 351 L 351
Cdd:PLN02586  351 I 351
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 33-351 2.43e-58

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 193.32  E-value: 2.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVGAQVFSCLECDRCKSDNEP 112
Cdd:PLN02178   31 ENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVG-KNVTKFKEGDRVGVGVIIGSCQSCESCNQDLEN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 113 YCTKFVTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCG--PGKKVGIVGLGG 190
Cdd:PLN02178  110 YCPKVVFTYNSRSSDGTRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTkeSGKRLGVNGLGG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 191 IGSMGTLISKAMGAETYVISRSSKKKEDAI-KMGADHYIATLEEGDWGEKYfDTFDLIVVCASSltdiDFNIMP--KAMK 267
Cdd:PLN02178  190 LGHIAVKIGKAFGLRVTVISRSSEKEREAIdRLGADSFLVTTDSQKMKEAV-GTMDFIIDTVSA----EHALLPlfSLLK 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 268 VGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEagVHEALERMERGDVRY 347
Cdd:PLN02178  265 VSGKLVALGLPEKPLDLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSD--INSAMDRLAKSDVRY 342


                  ....
gi 2507698970 348 RFTL 351
Cdd:PLN02178  343 RFVI 346
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 28-351 3.37e-56

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 186.59  E-value: 3.37e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNM-KMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFSCLECDRC 106
Cdd:cd08297    22 PEP-GPGEVLVKLEASGVCHTDLHAALGDWPVKpKLPLIGGHEGAGVVVAVGPGV-SGLKVGDRVGVKWLYDACGKCEYC 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGP------- 179
Cdd:cd08297   100 RTGDETLCPNQKNS-------GYTVDGTFAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYKALKKAGLKPgdwvvis 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 180 ------GkkvgivglggigSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYI---------ATLEEGDWGekyfdTF 244
Cdd:cd08297   173 gaggglG------------HLGVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVdfkksddveAVKELTGGG-----GA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 245 DLIVVCASSLTdiDFNIMPKAMKVGGRIVSISIPEQhEMLTLKPYG--LKAVSISYSALGSIKELKQLLALVSEKNIKVW 322
Cdd:cd08297   236 HAVVVTAVSAA--AYEQALDYLRPGGTLVCVGLPPG-GFIPLDPFDlvLRGITIVGSLVGTRQDLQEALEFAARGKVKPH 312

                         330       340
                  ....*....|....*....|....*....
gi 2507698970 323 VETLPVGEAGvhEALERMERGDVRYRFTL 351
Cdd:cd08297   313 IQVVPLEDLN--EVFEKMEEGKIAGRVVV 339
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 28-348 8.60e-56

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 185.53  E-value: 8.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVFSCLECDRCK 107
Cdd:cd08296    21 PLP-GPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGE-GVSRWKVGDRVGVGWHGGHCGTCDACR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 SDNepyctkFVTTYSQPYeDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVG 187
Cdd:cd08296    99 RGD------FVHCENGKV-TGVTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALRNSGAKPGDLVAVQG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 188 LGGIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATlEEGDWGEKYFDT--FDLIVVCASSltdidfnimPKA 265
Cdd:cd08296   172 IGGLGHLAVQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDT-SKEDVAEALQELggAKLILATAPN---------AKA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 266 M-------KVGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEAgvHEALE 338
Cdd:cd08296   242 IsalvgglAPRGKLLILGAAGEPVAVSPLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVETFPLEKA--NEAYD 319

                         330
                  ....*....|
gi 2507698970 339 RMERGDVRYR 348
Cdd:cd08296   320 RMMSGKARFR 329
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 27-346 2.61e-49

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 168.52  E-value: 2.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFSCLECDRC 106
Cdd:cd08298    26 EPGP---GEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGV-TRFSVGDRVGVPWLGSTCGECRYC 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08298   102 RSGRENLCDNARFT-------GYTVDGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALKLAGLKPGQRLGLY 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 GLGGIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGADhyiatlEEGDWGEKYFDTFDLIVVCASSltdidFNIMPKAM 266
Cdd:cd08298   175 GFGASAHLALQIARYQGAEVFAFTRSGEHQELARELGAD------WAGDSDDLPPEPLDAAIIFAPV-----GALVPAAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 267 KV---GGRIVS--ISIPEQHEMLTLKPYGLKavSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEAgvHEALERME 341
Cdd:cd08298   244 RAvkkGGRVVLagIHMSDIPAFDYELLWGEK--TIRSVANLTRQDGEEFLKLAAEIPIKPEVETYPLEEA--NEALQDLK 319


                  ....*
gi 2507698970 342 RGDVR 346
Cdd:cd08298   320 EGRIR 324
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 35-314 3.10e-49

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 166.34  E-value: 3.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAG-HWGNMKMPLVVGHEIVGKVVRLGDKsNSGLKVGQRVGVGAQVfSCLECDRCKsdnepy 113
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGgYPPPPKLPLILGHEGAGVVVEVGPG-VTGVKVGDRVVVLPNL-GCGTCELCR------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 114 ctkfvTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGC-GPGKKVGIVGlggIG 192
Cdd:cd05188    73 -----ELCPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVlKPGDTVLVLG---AG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 193 SMGTL---ISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFDT---FDLIVVCASSLTDIDFNImpKAM 266
Cdd:cd05188   145 GVGLLaaqLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGgggADVVIDAVGGPETLAQAL--RLL 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2507698970 267 KVGGRIVSISIPEQHEMLT-LKPYGLKAVSISYSALGSIKELKQLLALV 314
Cdd:cd05188   223 RPGGRIVVVGGTSGGPPLDdLRRLLFKELTIIGSTGGTREDFEEALDLL 271
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 27-345 5.37e-41

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 146.69  E-value: 5.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDhDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd08259    20 DPEPGPG-EVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVG-EGVERFKPGDRVILYYYIP-CGKCEYC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTkfvttysQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08259    97 LSGEENLCR-------NRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHALKRAGVKKGDTVLVT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 GLGGIGSMGTL-ISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFDTfDLIVVCASSLTdidFNIMPKA 265
Cdd:cd08259   170 GAGGGVGIHAIqLAKALGARVIAVTRSPEKLKILKELGADYVIDGSKFSEDVKKLGGA-DVVIELVGSPT---IEESLRS 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 266 MKVGGRIVSI--SIPEQHEmLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIK-VWVETLPVGEAGvhEALERMER 342
Cdd:cd08259   246 LNKGGRLVLIgnVTPDPAP-LRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKpVIDRVVSLEDIN--EALEDLKS 322


                  ...
gi 2507698970 343 GDV 345
Cdd:cd08259   323 GKV 325
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 35-352 1.16e-40

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 145.85  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGH-WGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAqVFSCLECDRCKSDNEPY 113
Cdd:cd08254    28 EVLVKVKAAGVCHSDLHILDGGvPTLTKLPLTLGHEIAGTVVEVGAGV-TNFKVGDRVAVPA-VIPCGACALCRRGRGNL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 114 CTKfvttysqPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGC-GPGKKVGIVGLGGIG 192
Cdd:cd08254   106 CLN-------QGMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEvKPGETVLVIGLGGLG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 193 SMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFD---TFDLIVVCASslTDIDFNIMPKAMKVG 269
Cdd:cd08254   179 LNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGlggGFDVIFDFVG--TQPTFEDAQKAVKPG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 270 GRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEagVHEALERMERGDVRYRF 349
Cdd:cd08254   257 GRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETRPLDE--IPEVLERLHKGKVKGRV 334


                  ...
gi 2507698970 350 TLI 352
Cdd:cd08254   335 VLV 337
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 27-344 1.23e-40

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 146.05  E-value: 1.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:COG1063    19 DPEP-GPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGV-TGLKVGDRV-VVEPNIPCGECRYC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYI-SQGGYANYVRVHEHFIVPIPENVPSHLAA---PLLCG-----------GLTVysp 171
Cdd:COG1063    96 RRGRYNLCENLQFL-------GIAgRDGGFAEYVRVPAANLVKVPDGLSDEAAAlvePLAVAlhaveragvkpGDTV--- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 172 LVrNGCGP-GkkvgivglggigSMGTLISKAMGAET-YVISRSSKKKEDAIKMGADHYIATLEEgDWGEKYFDT-----F 244
Cdd:COG1063   166 LV-IGAGPiG------------LLAALAARLAGAARvIVVDRNPERLELARELGADAVVNPREE-DLVEAVRELtggrgA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 245 DLIVVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNI---KV 321
Cdd:COG1063   232 DVVIEAVGA--PAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIdlePL 309

                         330       340
                  ....*....|....*....|...
gi 2507698970 322 WVETLPVGEAgvHEALERMERGD 344
Cdd:COG1063   310 ITHRFPLDDA--PEAFEAAADRA 330
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 27-352 1.39e-37

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 137.69  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGN---MKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAqVFSCLEC 103
Cdd:cd05284    20 VPEP-GPGQVLVRVGGAGVCHSDLHVIDGVWGGilpYKLPFTLGHENAGWVEEVGSGV-DGLKEGDPVVVHP-PWGCGTC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 104 DRCKSDNEPYCtkfvttySQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVR--NGCGPGK 181
Cdd:cd05284    97 RYCRRGEENYC-------ENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVKKalPYLDPGS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 182 KVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSKKKEDAIKMGADHYIATleEGDWGEKYFDT-----FDLIVVCASSLT 255
Cdd:cd05284   170 TVVVIGVGGLGHIAVQILRALTPATVIaVDRSEEALKLAERLGADHVLNA--SDDVVEEVRELtggrgADAVIDFVGSDE 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 256 DIDfnIMPKAMKVGGRIV------SISIPEQHEMltlkPYGlkaVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVG 329
Cdd:cd05284   248 TLA--LAAKLLAKGGRYVivgyggHGRLPTSDLV----PTE---ISVIGSLWGTRAELVEVVALAESGKVKVEITKFPLE 318

                         330       340
                  ....*....|....*....|...
gi 2507698970 330 EAgvHEALERMERGDVRYRFTLI 352
Cdd:cd05284   319 DA--NEALDRLREGRVTGRAVLV 339
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 34-352 2.42e-36

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 134.67  E-value: 2.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAGHW--GN----------MKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVfSCL 101
Cdd:cd08240    26 TEVLVKVTACGVCHSDLHIWDGGYdlGGgktmslddrgVKLPLVLGHEIVGEVVAVGP-DAADVKVGDKVLVYPWI-GCG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 102 ECDRCKSDNEPYCTKfvttysqPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYS----------- 170
Cdd:cd08240   104 ECPVCLAGDENLCAK-------GRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAYSavkklmplvad 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 171 -PLVRNGCGpgkkvgivglgGIGSMGTLISKAMG-AETYVISRSSKKKEDAIKMGADHYIatleegdWGEKYFDTFDLIV 248
Cdd:cd08240   177 ePVVIIGAG-----------GLGLMALALLKALGpANIIVVDIDEAKLEAAKAAGADVVV-------NGSDPDAAKRIIK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 249 VCASSLTD-IDF-NIMP------KAMKVGGRIV---------SISIPeqheMLTlkpygLKAVSISYSALGSIKELKQLL 311
Cdd:cd08240   239 AAGGGVDAvIDFvNNSAtaslafDILAKGGKLVlvglfggeaTLPLP----LLP-----LRALTIQGSYVGSLEELRELV 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2507698970 312 ALVSEKNIK-VWVETLPVGEagVHEALERMERGDVRYRFTLI 352
Cdd:cd08240   310 ALAKAGKLKpIPLTERPLSD--VNDALDDLKAGKVVGRAVLK 349
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 34-148 3.69e-35

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 124.26  E-value: 3.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVfSCLECDRCKSDNEPY 113
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGP-GVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2507698970 114 CTKFVTTysqpyedGYISQGGYANYVRVHEHFIVP 148
Cdd:pfam08240  79 CPNGRFL-------GYDRDGGFAEYVVVPERNLVP 106
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 35-347 6.61e-35

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 130.81  E-value: 6.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWgNMKMPLVVGHEIVGKVVRLGDKsNSGLKVGQRVGVgAQVFSCLECDRCKSDNEPYC 114
Cdd:cd08236    26 EVLVKVKACGICGSDIPRYLGTG-AYHPPLVLGHEFSGTVEEVGSG-VDDLAVGDRVAV-NPLLPCGKCEYCKKGEYSLC 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 115 TKFvttysqpyedGYI---SQGGYANYVRVHEHFIVPIPENVPSHLAA---PLLCGGLTVY-SPLVRN------GCGPgk 181
Cdd:cd08236   103 SNY----------DYIgsrRDGAFAEYVSVPARNLIKIPDHVDYEEAAmiePAAVALHAVRlAGITLGdtvvviGAGT-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 182 kvgivglggigsMGTLIS---KAMGAET-YVISRSSKKKEDAIKMGADHYIATLEEG-DWGEKYFD--TFDLIVVCASSL 254
Cdd:cd08236   171 ------------IGLLAIqwlKILGAKRvIAVDIDDEKLAVARELGADDTINPKEEDvEKVRELTEgrGADLVIEAAGSP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 255 TDIDFNIMpkAMKVGGRIVSISIPEQHEMLTLKPYG---LKAVSI-----SYSALGSIKELKQLLALVSEKNIKV---WV 323
Cdd:cd08236   239 ATIEQALA--LARPGGKVVLVGIPYGDVTLSEEAFEkilRKELTIqgswnSYSAPFPGDEWRTALDLLASGKIKVeplIT 316

                         330       340
                  ....*....|....*....|....
gi 2507698970 324 ETLPVGEAGvhEALERMERGDVRY 347
Cdd:cd08236   317 HRLPLEDGP--AAFERLADREEFS 338
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 27-346 2.70e-30

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 118.01  E-value: 2.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFyDHDVDIKIEACGVCGSDVHCAAGHWGNmKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd08234    19 VPEPG-PDEVLIKVAACGICGTDLHIYEGEFGA-APPLVPGHEFAGVVVAVGSKV-TGFKVGDRVAVDPNIY-CGECFYC 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKF----VTTysqpyedgyisQGGYANYVRVHEHFIVPIPENVPSHLAA---PLLC---G----GLTVYSPL 172
Cdd:cd08234    95 RRGRPNLCENLtavgVTR-----------NGGFAEYVVVPAKQVYKIPDNLSFEEAAlaePLSCavhGldllGIKPGDSV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 173 VRNGCGPgkkvgivglggigsMGTL---ISKAMGAETYVIS-RSSKKKEDAIKMGADHYIATLEE--GDWGEKYFDTFDl 246
Cdd:cd08234   164 LVFGAGP--------------IGLLlaqLLKLNGASRVTVAePNEEKLELAKKLGATETVDPSREdpEAQKEDNPYGFD- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 247 IVVCASSLTDIdFNIMPKAMKVGGRIVSISIPEQHEMLTLKPYGL--KAVSI--SYSALGSIkelKQLLALVSEKNIKVW 322
Cdd:cd08234   229 VVIEATGVPKT-LEQAIEYARRGGTVLVFGVYAPDARVSISPFEIfqKELTIigSFINPYTF---PRAIALLESGKIDVK 304

                         330       340
                  ....*....|....*....|....*..
gi 2507698970 323 V---ETLPVGEagVHEALERMERGDVR 346
Cdd:cd08234   305 GlvsHRLPLEE--VPEALEGMRSGGAL 329
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 27-228 1.30e-29

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 116.55  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVGAqVFSCLECDRC 106
Cdd:cd08260    20 DPEP-PPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVG-EDVSRWRVGDRVTVPF-VLGCGTCPYC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCtkfvTTYSQPyedGYISQGGYANYVRVH--EHFIVPIPENVPSHLAAPLLCGGLTVYSPLV-RNGCGPGKKV 183
Cdd:cd08260    97 RAGDSNVC----EHQVQP---GFTHPGSFAEYVAVPraDVNLVRLPDDVDFVTAAGLGCRFATAFRALVhQARVKPGEWV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2507698970 184 GIVGLGGIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYI 228
Cdd:cd08260   170 AVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGAVATV 214
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 38-345 4.76e-29

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 115.05  E-value: 4.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  38 IKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLG-----DKSNSGLKVGQRVgVGAQVFSCLECDRCK-SDNE 111
Cdd:cd08231    30 VRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGggvttDVAGEPLKVGDRV-TWSVGAPCGRCYRCLvGDPT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 112 PYCTKFVTTYSQPYEDGYISqGGYANYVRVH-EHFIVPIPENVPSHLAAPLLCGGLTVYSPL------------VRNGCG 178
Cdd:cd08231   109 KCENRKKYGHEASCDDPHLS-GGYAEHIYLPpGTAIVRVPDNVPDEVAAPANCALATVLAALdragpvgagdtvVVQGAG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 179 PgkkvgivglggigsMG---TLISKAMGAE-TYVISRSSKKKEDAIKMGADHYIATLEEGDWGEK-------YFDTFDLI 247
Cdd:cd08231   188 P--------------LGlyaVAAAKLAGARrVIVIDGSPERLELAREFGADATIDIDELPDPQRRaivrditGGRGADVV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 248 VVCASSLTDIDFNIMpkAMKVGGRIVSISIPEQHEMLTLKPYGL--KAVSISYSALGSIKELKQLLALVSEKNIKV-WVE 324
Cdd:cd08231   254 IEASGHPAAVPEGLE--LLRRGGTYVLVGSVAPAGTVPLDPERIvrKNLTIIGVHNYDPSHLYRAVRFLERTQDRFpFAE 331

                         330       340
                  ....*....|....*....|...
gi 2507698970 325 --TLPVGEAGVHEALERMERGDV 345
Cdd:cd08231   332 lvTHRYPLEDINEALELAESGTA 354
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 27-346 6.25e-29

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 114.09  E-value: 6.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNM-KMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGvgaqvfsclecdr 105
Cdd:COG0604    24 EPGP---GEVLVRVKAAGVNPADLLIRRGLYPLPpGLPFIPGSDAAGVVVAVGEGV-TGFKVGDRVA------------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 cksdnepyctkfvttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRN---------- 175
Cdd:COG0604    87 ----------------------GLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRgrlkpgetvl 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 176 ------GCGpgkkvgivglggigSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATlEEGDWGEK-----YFDTF 244
Cdd:COG0604   145 vhgaagGVG--------------SAAVQLAKALGARVIATASSPEKAELLRALGADHVIDY-REEDFAERvraltGGRGV 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 245 DLIV--VCASSLTDIdfnimPKAMKVGGRIVSI-SIPEQHEMLTLKPYGLKAVSISYSALGSI------KELKQLLALVS 315
Cdd:COG0604   210 DVVLdtVGGDTLARS-----LRALAPGGRLVSIgAASGAPPPLDLAPLLLKGLTLTGFTLFARdpaerrAALAELARLLA 284

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2507698970 316 EKNIKVWV-ETLPVGEAGvhEALERMERGDVR 346
Cdd:COG0604   285 AGKLRPVIdRVFPLEEAA--EAHRLLESGKHR 314
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 27-343 1.70e-28

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 113.21  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDhDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:PRK13771   20 DPKPGKD-EVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENV-KGFKPGDRV-ASLLYAPDGTCEYC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCtkfvttysqPYEDGYIS--QGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVG 184
Cdd:PRK13771   97 RSGEEAYC---------KNRLGYGEelDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGLRRAGVKKGETVL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 185 IVGLGGIGSMGTL-ISKAMGAeTYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFDTfDLIVVCASSLTdidFNIMP 263
Cdd:PRK13771  168 VTGAGGGVGIHAIqVAKALGA-KVIAVTSSESKAKIVSKYADYVIVGSKFSEEVKKIGGA-DIVIETVGTPT---LEESL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 264 KAMKVGGRIVSIS--IPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKvwvetlPVgeAGVHEALERME 341
Cdd:PRK13771  243 RSLNMGGKIIQIGnvDPSPTYSLRLGYIILKDIEIIGHISATKRDVEEALKLVAEGKIK------PV--IGAEVSLSEID 314


                  ..
gi 2507698970 342 RG 343
Cdd:PRK13771  315 KA 316
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 35-321 1.72e-28

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 113.46  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVgAQVFSCLECDRCKSDNEPYC 114
Cdd:cd08235    26 EVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGV-TGFKVGDRVFV-APHVPCGECHYCLRGNENMC 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 115 TKFvttysqpYEDGYISQGGYANYVRVHEHF-----IVPIPENVPSHLAA---PLLCggltVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08235   104 PNY-------KKFGNLYDGGFAEYVRVPAWAvkrggVLKLPDNVSFEEAAlvePLAC----CINAQRKAGIKPGDTVLVI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 GLGGIGSMGTLISKAMGAETYVIS-RSSKKKEDAIKMGADHYIATLEEgDWGEKYFDT-----FDLIVVCASSLTDIDFN 260
Cdd:cd08235   173 GAGPIGLLHAMLAKASGARKVIVSdLNEFRLEFAKKLGADYTIDAAEE-DLVEKVRELtdgrgADVVIVATGSPEAQAQA 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507698970 261 ImpKAMKVGGRIVSISIPEQHEMLTLKP----YGLKAVSISYSAlgSIKELKQLLALVSEKNIKV 321
Cdd:cd08235   252 L--ELVRKGGRILFFGGLPKGSTVNIDPnlihYREITITGSYAA--SPEDYKEALELIASGKIDV 312
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 18-321 1.01e-27

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 111.48  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  18 WKNPKKTKYD---PKPFYDHDVDIKIEACGVCGSDVH-----------CAAGHWGNMKMPLVVGHEIVGKVVRLGDKSNs 83
Cdd:cd08233     6 YHGRKDIRVEevpEPPVKPGEVKIKVAWCGICGSDLHeyldgpifiptEGHPHLTGETAPVTLGHEFSGVVVEVGSGVT- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  84 GLKVGQRVGVGAqVFSCLECDRCKSDNEPYCTKFvttysqpyedGYI----SQGGYANYVRVHEHFIVPIPENVPSHLAA 159
Cdd:cd08233    85 GFKVGDRVVVEP-TIKCGTCGACKRGLYNLCDSL----------GFIglggGGGGFAEYVVVPAYHVHKLPDNVPLEEAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 160 ---PL-------LCGGLTVYSPLVRNGCGP-GkkvgivglggigsMGT-LISKAMGAETYVISR-SSKKKEDAIKMGADH 226
Cdd:cd08233   154 lvePLavawhavRRSGFKPGDTALVLGAGPiG-------------LLTiLALKAAGASKIIVSEpSEARRELAEELGATI 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 227 YIATLEEGDW-------GEKYFD-TFDlivvCASSltDIDFNIMPKAMKVGGRIVSISIPEQ----HEM-LTLKPYGLKA 293
Cdd:cd08233   221 VLDPTEVDVVaevrkltGGGGVDvSFD----CAGV--QATLDTAIDALRPRGTAVNVAIWEKpisfNPNdLVLKEKTLTG 294

                         330       340
                  ....*....|....*....|....*...
gi 2507698970 294 vSISYSAlgsiKELKQLLALVSEKNIKV 321
Cdd:cd08233   295 -SICYTR----EDFEEVIDLLASGKIDA 317
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 28-300 1.54e-27

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 110.10  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFSCLECDRCK 107
Cdd:cd08258    22 PEP-GPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDV-EGWKVGDRVVSETTFSTCGRCPYCR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 SDNEPYCTKFVTtysqpyeDGYISQGGYANYVRVHEHFIVPIPENVPSHLAA---PLLCGGLTVYSP-LVRNG-----CG 178
Cdd:cd08258   100 RGDYNLCPHRKG-------IGTQADGGFAEYVLVPEESLHELPENLSLEAAAltePLAVAVHAVAERsGIRPGdtvvvFG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 179 PGkkvgivglggigSMGTL---ISKAMGAETYVISRSSKKKEDAI--KMGADHYIATLE---EGDWGEKYFDTFDLIVVC 250
Cdd:cd08258   173 PG------------PIGLLaaqVAKLQGATVVVVGTEKDEVRLDVakELGADAVNGGEEdlaELVNEITDGDGADVVIEC 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507698970 251 ASSLtdIDFNIMPKAMKVGGRIVSISI-PEQHEMLTLKPYGLKAVSI--SYSA 300
Cdd:cd08258   241 SGAV--PALEQALELLRKGGRIVQVGIfGPLAASIDVERIIQKELSVigSRSS 291
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 27-356 1.72e-27

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 110.51  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNmKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVGVGAQVFSCLECDRC 106
Cdd:PRK09422   19 TLRPLKHGEALVKMEYCGVCHTDLHVANGDFGD-KTGRILGHEGIGIVKEVGPGVTS-LKVGDRVSIAWFFEGCGHCEYC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIV 186
Cdd:PRK09422   97 TTGRETLCRSVKNA-------GYTVDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTTYKAIKVSGIKPGQWIAIY 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 GLggiGSMGTL----ISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFDTF---DLIVVCASSltDIDF 259
Cdd:PRK09422  170 GA---GGLGNLalqyAKNVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQEKTggaHAAVVTAVA--KAAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 260 NIMPKAMKVGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWVETLPVGEagVHEALER 339
Cdd:PRK09422  245 NQAVDAVRAGGRVVAVGLPPESMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLED--INDIFDE 322

                         330
                  ....*....|....*..
gi 2507698970 340 MERGDVRYRFtLIDYDK 356
Cdd:PRK09422  323 MEQGKIQGRM-VIDFTH 338
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 27-339 7.84e-26

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 105.51  E-value: 7.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNmKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd08264    21 DPKP-GPGEVLIRVKMAGVNPVDYNVINAVKVK-PMPHIPGAEFAGVVEEVGDHV-KGVKKGDRVVVYNRVF-DGTCDMC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCtkfvttysqpyEDGYI----SQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKK 182
Cdd:cd08264    97 LSGNEMLC-----------RNGGIigvvSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAGLGPGET 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 183 VGIVGLGGIGSMGTL-ISKAMGAETYVISRSSKKKEdaikMGADH---YIATLEEGDWGEKYFDtfdlIVV--CASSLTD 256
Cdd:cd08264   166 VVVFGASGNTGIFAVqLAKMMGAEVIAVSRKDWLKE----FGADEvvdYDEVEEKVKEITKMAD----VVInsLGSSFWD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 257 IDFnimpKAMKVGGRIVSISIPEQHEM-LTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWvETLPVGEAgvHE 335
Cdd:cd08264   238 LSL----SVLGRGGRLVTFGTLTGGEVkLDLSDLYSKQISIIGSTGGTRKELLELVKIAKDLKVKVW-KTFKLEEA--KE 310


                  ....
gi 2507698970 336 ALER 339
Cdd:cd08264   311 ALKE 314
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 38-233 5.87e-25

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 103.99  E-value: 5.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  38 IKIEACGVCGSDVHCAAGHWGnMKMPLVVGHEIVGKVVRLGD--KSNSGLKVGQRVgVGAQVFSCLECDRCKSDNEPYCT 115
Cdd:cd08263    30 IRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGPnvENPYGLSVGDRV-VGSFIMPCGKCRYCARGKENLCE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 116 KFVT-----------TYSQPYEDG---YI-SQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNG-CGP 179
Cdd:cd08263   108 DFFAynrlkgtlydgTTRLFRLDGgpvYMySMGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAAdVRP 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2507698970 180 GKKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSKKKEDAIKMGADHYIATLEE 233
Cdd:cd08263   188 GETVAVIGVGGVGSSAIQLAKAFGASPIIaVDVRDEKLAKAKELGATHTVNAAKE 242
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 28-346 7.97e-24

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 99.94  E-value: 7.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFyDHDVDIKIEACGVCGSDVHCAAGHWGNM---KMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgvgaqvfsclecd 104
Cdd:cd05289    23 PEPG-PGEVLVKVHAAGVNPVDLKIREGLLKAAfplTLPLIPGHDVAGVVVAVGPGV-TGFKVGDEV------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 105 rcksdnepyctkfvttYSQPYEDGyisQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGC-GPGKKV 183
Cdd:cd05289    88 ----------------FGMTPFTR---GGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGlKAGQTV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 184 givglggigsmgtLIS--------------KAMGAetYVISRSSKKKEDAIK-MGADHYIATLEEGDWGEKYFDTFDLIV 248
Cdd:cd05289   149 -------------LIHgaaggvgsfavqlaKARGA--RVIATASAANADFLRsLGADEVIDYTKGDFERAAAPGGVDAVL 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 249 VCASSLTDIDFnimPKAMKVGGRIVSISIPEQHEmLTLKPYGLKAVSISYSALGsiKELKQLLALVSEKNIKVWV-ETLP 327
Cdd:cd05289   214 DTVGGETLARS---LALVKPGGRLVSIAGPPPAE-QAAKRRGVRAGFVFVEPDG--EQLAELAELVEAGKLRPVVdRVFP 287

                         330
                  ....*....|....*....
gi 2507698970 328 VGEAgvHEALERMERGDVR 346
Cdd:cd05289   288 LEDA--AEAHERLESGHAR 304
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 27-291 1.41e-22

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 97.23  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMkMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:cd08279    22 DPGP---GEVLVRIAAAGLCHSDLHVVTGDLPAP-LPAVLGHEGAGVVEEVGPGV-TGVKPGDHV-VLSWIPACGTCRYC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTYSQPYEDG--YISQGG-----------YANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT-----V 168
Cdd:cd08279    96 SRGQPNLCDLGAGILGGQLPDGtrRFTADGepvgamcglgtFAEYTVVPEASVVKIDDDIPLDRAALLGCGVTTgvgavV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 169 YSPLVRN-------GCGpgkkvgivglggigsmGTLISKAMGAetyVISRSSK---------KKEDAIKMGADHYIATLE 232
Cdd:cd08279   176 NTARVRPgdtvaviGCG----------------GVGLNAIQGA---RIAGASRiiavdpvpeKLELARRFGATHTVNASE 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507698970 233 E----------GDWGekyfdtFDLIVVCASSLTDID--FNIMPKamkvGGRIVSISIPEQHEMLTLKPYGL 291
Cdd:cd08279   237 DdaveavrdltDGRG------ADYAFEAVGRAATIRqaLAMTRK----GGTAVVVGMGPPGETVSLPALEL 297
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 28-287 2.68e-22

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 96.05  E-value: 2.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFYDH-DVDIKIEACGVCGSDVHCAAghW-----GNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRV-GVGAQVfsC 100
Cdd:PRK05396   19 PVPEPGPnDVLIKVKKTAICGTDVHIYN--WdewaqKTIPVPMVVGHEFVGEVVEVG-SEVTGFKVGDRVsGEGHIV--C 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 101 LECDRCKSDNEPYC--TKFVttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAA---PL-------LCGGLTV 168
Cdd:PRK05396   94 GHCRNCRAGRRHLCrnTKGV---------GVNRPGAFAEYLVIPAFNVWKIPDDIPDDLAAifdPFgnavhtaLSFDLVG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 169 YSPLVrNGCGP-GkkvgivglggigSMGTLISKAMGAETYVISRSSKKKED-AIKMGADHYIATLEEG------DWGEKY 240
Cdd:PRK05396  165 EDVLI-TGAGPiG------------IMAAAVAKHVGARHVVITDVNEYRLElARKMGATRAVNVAKEDlrdvmaELGMTE 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2507698970 241 -FDtfdliVVCASSLTDIDFNIMPKAMKVGGRIVSISIPEQH----------EMLTLK 287
Cdd:PRK05396  232 gFD-----VGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPGDmaidwnkvifKGLTIK 284
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 27-230 7.11e-22

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 94.69  E-value: 7.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDhDVDIKIEACGVCGSDVHC-AAGHWGNMKMPLVVGHEIVGKVVRLGDKSNSGlKVGQRVGVGAQVFsCLECDR 105
Cdd:cd08239    19 VPVPGPG-EVLLRVKASGLCGSDLHYyYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHF-RVGDRVMVYHYVG-CGACRN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 CKSDNEPYCTKFVTTYsqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGI 185
Cdd:cd08239    96 CRRGWMQLCTSKRAAY------GWNRDGGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALRRVGVSGRDTVLV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2507698970 186 VGLGGIGSMGTLISKAMGAET-YVISRSSKKKEDAIKMGADHYIAT 230
Cdd:cd08239   170 VGAGPVGLGALMLARALGAEDvIGVDPSPERLELAKALGADFVINS 215
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 38-224 7.32e-22

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 94.60  E-value: 7.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  38 IKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVGAQVFSCLECDRCKSDNEPYCTKf 117
Cdd:TIGR02822  32 VRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRG-ADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAENLCPA- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 118 vTTYSqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTL 197
Cdd:TIGR02822 110 -SRYT-----GWDTDGGYAEYTTVPAAFAYRLPTGYDDVELAPLLCAGIIGYRALLRASLPPGGRLGLYGFGGSAHLTAQ 183

                         170       180
                  ....*....|....*....|....*..
gi 2507698970 198 ISKAMGAETYVISRSSKKKEDAIKMGA 224
Cdd:TIGR02822 184 VALAQGATVHVMTRGAAARRLALALGA 210
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 28-279 1.14e-21

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 94.22  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDVHC------AAGHwgnMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVfSCL 101
Cdd:cd05281    21 PKP-GPGEVLIKVLAASICGTDVHIyewdewAQSR---IKPPLIFGHEFAGEVVEVGEGV-TRVKVGDYVSAETHI-VCG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 102 ECDRCKSDNEPYC--TKFVttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAA---PL-------LCGGLTVY 169
Cdd:cd05281    95 KCYQCRTGNYHVCqnTKIL---------GVDTDGCFAEYVVVPEENLWKNDKDIPPEIASiqePLgnavhtvLAGDVSGK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 170 SPLVrNGCGPgkkvgivglggIGSMGTLISKAMGAET-YVISRSSKKKEDAIKMGADHYIATLEEgDWGEKYfDTFDLI- 247
Cdd:cd05281   166 SVLI-TGCGP-----------IGLMAIAVAKAAGASLvIASDPNPYRLELAKKMGADVVINPREE-DVVEVK-SVTDGTg 231

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2507698970 248 --VVCASSLTDIDFNIMPKAMKVGGRIVSISIPE 279
Cdd:cd05281   232 vdVVLEMSGNPKAIEQGLKALTPGGRVSILGLPP 265
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 33-275 1.78e-20

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 90.76  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACGVCGSDVHCAA-GHWGN--MKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVfSCLECDRCKSD 109
Cdd:cd08232    21 PGEVRVRVAAGGICGSDLHYYQhGGFGTvrLREPMVLGHEVSGVVEAVGP-GVTGLAPGQRVAVNPSR-PCGTCDYCRAG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 110 NEPYCT--KFVTTYSQ-PYEdgyisQGGYANYVRVHEHFIVPIPENVPSHLAA---PL--------LCGGLTVYSPLVrN 175
Cdd:cd08232    99 RPNLCLnmRFLGSAMRfPHV-----QGGFREYLVVDASQCVPLPDGLSLRRAAlaePLavalhavnRAGDLAGKRVLV-T 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 176 GCGPgkkvgivglggigsMGTLI---SKAMGAETYVISR-SSKKKEDAIKMGADHYI-ATLEEGDWGEKYFDTFDLIVVC 250
Cdd:cd08232   173 GAGP--------------IGALVvaaARRAGAAEIVATDlADAPLAVARAMGADETVnLARDPLAAYAADKGDFDVVFEA 238

                         250       260
                  ....*....|....*....|....*
gi 2507698970 251 ASSLTDIDFNImpKAMKVGGRIVSI 275
Cdd:cd08232   239 SGAPAALASAL--RVVRPGGTVVQV 261
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 27-167 1.36e-19

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 88.71  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMkMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGaqvF-SCLECDR 105
Cdd:cd08278    24 DPRP---DEVLVRIVATGICHTDLVVRDGGLPTP-LPAVLGHEGAGVVEAVGSAV-TGLKPGDHVVLS---FaSCGECAN 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2507698970 106 CKSDNEPYCTKFV------------TTYSQPYEDGYIS----QGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT 167
Cdd:cd08278    96 CLSGHPAYCENFFplnfsgrrpdgsTPLSLDDGTPVHGhffgQSSFATYAVVHERNVVKVDKDVPLELLAPLGCGIQT 173
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 27-345 2.61e-19

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 87.70  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDhDVDIKIEACGVCGSDVHCAAGHWG-NMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVfSCLECDR 105
Cdd:cd08266    22 EPEPGPD-EVLVRVKAAALNHLDLWVRRGMPGiKLPLPHILGSDGAGVVEAVGPGV-TNVKPGQRVVIYPGI-SCGRCEY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 CKSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRN---------- 175
Cdd:cd08266    99 CLAGRENLCAQYGIL-------GEHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRarlrpgetvl 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 176 --GCGPGkkvgivglggIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIaTLEEGDWGEKYFD-TF----DLIV 248
Cdd:cd08266   172 vhGAGSG----------VGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVI-DYRKEDFVREVRElTGkrgvDVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 249 VCASSLTdidFNIMPKAMKVGGRIVSI-----SIPEqhemLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIKVWV 323
Cdd:cd08266   241 EHVGAAT---WEKSLKSLARGGRLVTCgattgYEAP----IDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPVI 313

                         330       340
                  ....*....|....*....|...
gi 2507698970 324 ET-LPVGEAgvHEALERMERGDV 345
Cdd:cd08266   314 DSvFPLEEA--AEAHRRLESREQ 334
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 28-275 3.04e-19

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 87.55  E-value: 3.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDVH-CAAGHWGNM--KMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVFsCLECD 104
Cdd:cd05285    18 PEP-GPGEVLVRVRAVGICGSDVHyYKHGRIGDFvvKEPMVLGHESAGTVVAVGS-GVTHLKVGDRVAIEPGVP-CRTCE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 105 RCKSDNEPYC--TKFVTTysQPYedgyisQGGYANYVRVHEHFIVPIPENVPSHLAA---PLLCG-------GLTVYSPL 172
Cdd:cd05285    95 FCKSGRYNLCpdMRFAAT--PPV------DGTLCRYVNHPADFCHKLPDNVSLEEGAlvePLSVGvhacrraGVRPGDTV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 173 VRNGCGP-GkkvgivglggigSMGTLISKAMGAETYVISRSSKKK-EDAIKMGADHYI-----ATLEEGDWGEKYFDT-- 243
Cdd:cd05285   167 LVFGAGPiG------------LLTAAVAKAFGATKVVVTDIDPSRlEFAKELGATHTVnvrteDTPESAEKIAELLGGkg 234

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2507698970 244 FDLIVVCASSLTDIDFNImpKAMKVGGRIVSI 275
Cdd:cd05285   235 PDVVIECTGAESCIQTAI--YATRPGGTVVLV 264
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 27-339 8.90e-19

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 86.21  E-value: 8.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFyDHDVDIKIEACGVCGSDVHCAAG-------HWGNMKM----PLVVGHEIVGKVVRLGDKSNSGLKVGQRVgVGA 95
Cdd:cd08262    18 DPEPG-PGQVLVKVLACGICGSDLHATAHpeamvddAGGPSLMdlgaDIVLGHEFCGEVVDYGPGTERKLKVGTRV-TSL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  96 QVFSCLECDRCKsdnepyCTKFVTTYsqpyedgyisqGGYANYVRVHEHFIVPIPENVPSHLAA---PL--------LCG 164
Cdd:cd08262    96 PLLLCGQGASCG------IGLSPEAP-----------GGYAEYMLLSEALLLRVPDGLSMEDAAltePLavglhavrRAR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 165 GLTVYSPLVRnGCGPgkkvgivglggigsMG---TLISKAMGAETYVIS-RSSKKKEDAIKMGADHYI---ATLEEGDWG 237
Cdd:cd08262   159 LTPGEVALVI-GCGP--------------IGlavIAALKARGVGPIVASdFSPERRALALAMGADIVVdpaADSPFAAWA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 238 EKYFDTF----DLIVVCASSLTDIDFNImpKAMKVGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLAL 313
Cdd:cd08262   224 AELARAGgpkpAVIFECVGAPGLIQQII--EGAPPGGRIVVVGVCMESDNIEPALAIRKELTLQFSLGYTPEEFADALDA 301

                         330       340
                  ....*....|....*....|....*..
gi 2507698970 314 VSEKNIKVW-VETLPVGEAGVHEALER 339
Cdd:cd08262   302 LAEGKVDVApMVTGTVGLDGVPDAFEA 328
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 33-242 9.17e-19

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 85.89  E-value: 9.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACGVCGSDVHC-AAGHWGN--MKMPLVVGHEIVGKVVrlgDKSNSGLKVGQRVGVGAQVfSCLECDRCKSD 109
Cdd:PRK09880   27 NNGTLVQITRGGICGSDLHYyQEGKVGNfvIKAPMVLGHEVIGKIV---HSDSSGLKEGQTVAINPSK-PCGHCKYCLSH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 110 NEPYCTK---FVTTYSQPYEDgyisqGGYANYVRVHEHFIVPIPENVPSHL---AAPL--------LCGGLTVYSPLVrN 175
Cdd:PRK09880  103 NENQCTTmrfFGSAMYFPHVD-----GGFTRYKVVDTAQCIPYPEKADEKVmafAEPLavaihaahQAGDLQGKRVFV-S 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507698970 176 GCGPgkkvgivglggigsMGTLI---SKAMGAETYVISRSSKKKED-AIKMGADHYIATLEE--GDWGEK--YFD 242
Cdd:PRK09880  177 GVGP--------------IGCLIvaaVKTLGAAEIVCADVSPRSLSlAREMGADKLVNPQNDdlDHYKAEkgYFD 237
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
193-316 2.55e-18

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 79.96  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 193 SMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATlEEGDWGEKYFD-T----FDLIVVCASSltDIDFNIMPKAMK 267
Cdd:pfam00107   4 LAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINP-KETDLVEEIKElTggkgVDVVFDCVGS--PATLEQALKLLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2507698970 268 VGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSE 316
Cdd:pfam00107  81 PGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 27-345 1.88e-16

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 79.08  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGN-MKMPLVVGHEIVGKVVRLGDKsNSGLKVGQRVGVGAQvfsclecdr 105
Cdd:cd08241    21 PPEPGAPGEVRIRVEAAGVNFPDLLMIQGKYQVkPPLPFVPGSEVAGVVEAVGEG-VTGFKVGDRVVALTG--------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 cksdnepyctkfvttysqpyedgyisQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGC-GPGKkvg 184
Cdd:cd08241    91 --------------------------QGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARlQPGE--- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 185 ivglggigsmgTL---------------ISKAMGAETYVISRSSKKKEDAIKMGADHYIaTLEEGDWGEKYFDTF----- 244
Cdd:cd08241   142 -----------TVlvlgaaggvglaavqLAKALGARVIAAASSEEKLALARALGADHVI-DYRDPDLRERVKALTggrgv 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 245 DLIV------VCASSLtdidfnimpKAMKVGGRIVSI-----SIPEQHEMLTLkpygLKAVSI------SYSAL---GSI 304
Cdd:cd08241   210 DVVYdpvggdVFEASL---------RSLAWGGRLLVIgfasgEIPQIPANLLL----LKNISVvgvywgAYARRepeLLR 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2507698970 305 KELKQLLALVSEKNIKVWV-ETLPVGEAGvhEALERMERGDV 345
Cdd:cd08241   277 ANLAELFDLLAEGKIRPHVsAVFPLEQAA--EALRALADRKA 316
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 27-320 3.12e-16

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 78.86  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd05278    19 DPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKR-LKPGDRVSVPCITF-CGRCRFC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTkfvTTYSQPYeDGYISQGGYANYVRVHE--HFIVPIPENVPshLAAPLLCG-----------------GLT 167
Cdd:cd05278    97 RRGYHAHCE---NGLWGWK-LGNRIDGGQAEYVRVPYadMNLAKIPDGLP--DEDALMLSdilptgfhgaelagikpGST 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 168 VYspLVrnGCGPgkkvgivglggIGSMGTLISKAMGAE-TYVISRSSKKKEDAIKMGADhYIATLEEGDWGEKYFDT--- 243
Cdd:cd05278   171 VA--VI--GAGP-----------VGLCAVAGARLLGAArIIAVDSNPERLDLAKEAGAT-DIINPKNGDIVEQILELtgg 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 244 --FDLIVVCASSLTdiDFNIMPKAMKVGGRIVSISIPEQHEMLTLK-PYGLKAVSISYSALGSIKELKQLLALVSEKNIK 320
Cdd:cd05278   235 rgVDCVIEAVGFEE--TFEQAVKVVRPGGTIANVGVYGKPDPLPLLgEWFGKNLTFKTGLVPVRARMPELLDLIEEGKID 312
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 34-163 1.99e-15

Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 76.29  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHC---AAGHWGN------MKMPLVVGHEIVGKVVRLG-DKSNSGLKVGQRVgVGAQVFSCLEC 103
Cdd:cd08256    25 GEILVKVEACGICAGDIKCyhgAPSFWGDenqppyVKPPMIPGHEFVGRVVELGeGAEERGVKVGDRV-ISEQIVPCWNC 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2507698970 104 DRCKSDNEPYCTKfvttysqpyEDGYISQ----GGYANYVRVHEHFIV-PIPENVPSHLAA---PLLC 163
Cdd:cd08256   104 RFCNRGQYWMCQK---------HDLYGFQnnvnGGMAEYMRFPKEAIVhKVPDDIPPEDAIliePLAC 162
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 18-345 2.36e-15

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 76.14  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  18 WKNPKKTKY----DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKmPLVVGHEIVGKVVRLGDkSNSGLKVGQRVgV 93
Cdd:cd08284     6 FKGPGDVRVeevpIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIPSTP-GFVLGHEFVGEVVEVGP-EVRTLKVGDRV-V 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  94 GAQVFSCLECDRCKSDNEPYCTK---FVTTYSQPYedgyisQGGYANYVRV--HEHFIVPIPENVPSHLAapLLCG---- 164
Cdd:cd08284    83 SPFTIACGECFYCRRGQSGRCAKgglFGYAGSPNL------DGAQAEYVRVpfADGTLLKLPDGLSDEAA--LLLGdilp 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 165 -------------GLTVysplVRNGCGP-GKkvgivglggigsMGTLISKAMGAET-YVISRSSKKKEDAIKMGA----- 224
Cdd:cd08284   155 tgyfgakraqvrpGDTV----AVIGCGPvGL------------CAVLSAQVLGAARvFAVDPVPERLERAAALGAepinf 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 225 -----DHYIATLEEGdwgekyfDTFDLI--VVCASSLTDIDFNIMPKamkvGGRIVSISIPEQHEM-LTLKPYGLKAVSI 296
Cdd:cd08284   219 edaepVERVREATEG-------RGADVVleAVGGAAALDLAFDLVRP----GGVISSVGVHTAEEFpFPGLDAYNKNLTL 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2507698970 297 SYSALGSIKELKQLLALVSEKNIKVWV---ETLPVGEAGvhEALERMERGDV 345
Cdd:cd08284   288 RFGRCPVRSLFPELLPLLESGRLDLEFlidHRMPLEEAP--EAYRLFDKRKV 337
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 18-346 4.12e-15

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 75.63  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  18 WKNPK---KTKYDPKPfYDHDVDIKIEACGVCGSDVHCAAG-------HWGNMKMPLVVGHEIVGKVVRLGdKSNSGLKV 87
Cdd:cd08265    34 WRYPElrvEDVPVPNL-KPDEILIRVKACGICGSDIHLYETdkdgyilYPGLTEFPVVIGHEFSGVVEKTG-KNVKNFEK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  88 GQRVgVGAQVFSCLECDRCKSDNEPYCTKFvttysqpYEDGYISQGGYANYVRVHEHF------IVPIPENVPSHLAAPL 161
Cdd:cd08265   112 GDPV-TAEEMMWCGMCRACRSGSPNHCKNL-------KELGFSADGAFAEYIAVNARYaweineLREIYSEDKAFEAGAL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 162 LCGGLTVYSPLVRNGCG--PGKKVGIVGLGGIGSMGTLISKAMGAETYVISR-SSKKKEDAIKMGADHYIATLEEGD--- 235
Cdd:cd08265   184 VEPTSVAYNGLFIRGGGfrPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEiSEERRNLAKEMGADYVFNPTKMRDcls 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 236 ----------WGEKYFdtfdlivVCASSLTDIDFNIMPKAMKVGGRIVSISIPEQHEMLTLKPYGLKAVSI----SYSAL 301
Cdd:cd08265   264 gekvmevtkgWGADIQ-------VEAAGAPPATIPQMEKSIAINGKIVYIGRAATTVPLHLEVLQVRRAQIvgaqGHSGH 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2507698970 302 GSIKELKQLLALVSEKNIKVWVETLPvgEAGVHEALERM-ERGDVR 346
Cdd:cd08265   337 GIFPSVIKLMASGKIDMTKIITARFP--LEGIMEAIKAAsERTDGK 380
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 28-277 5.65e-15

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 74.92  E-value: 5.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKP-FYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:cd08261    18 PEPvPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGV-AGLKVGDRV-VVDPYISCGECYAC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 KSDNEPYCTKFVTTysqpyedGYISQGGYANYVRVHEHFiVPIPENVPSHLAA---PLLCGGLTVYsplvRNGCGPGKKV 183
Cdd:cd08261    96 RKGRPNCCENLQVL-------GVHRDGGFAEYIVVPADA-LLVPEGLSLDQAAlvePLAIGAHAVR----RAGVTAGDTV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 184 GIVGlggigsMG------TLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEgDWGEKYF-----DTFDLIV--VC 250
Cdd:cd08261   164 LVVG------AGpiglgvIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDE-DVAARLReltdgEGADVVIdaTG 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 2507698970 251 ASSltdidfnIMPKAMKV---GGRIVSISI 277
Cdd:cd08261   237 NPA-------SMEEAVELvahGGRVVLVGL 259
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-346 6.55e-15

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 74.56  E-value: 6.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFyDHDVDIKIEACGVCGSDVHCAAGHWGNM---KMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVgvgaqvFSCLECD 104
Cdd:cd08267    22 PTPK-PGEVLVKVHAASVNPVDWKLRRGPPKLLlgrPFPPIPGMDFAGEVVAVG-SGVTRFKVGDEV------FGRLPPK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 105 RcksdnepyctkfvttysqpyedgyisQGGYANYVRVHEHFIVPIPENVpSHL-AAPLLCGGLTVYSPLVRN-------- 175
Cdd:cd08267    94 G--------------------------GGALAEYVVAPESGLAKKPEGV-SFEeAAALPVAGLTALQALRDAgkvkpgqr 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 176 --------GCGpgkkvgivglggigSMGTLISKAMGAEtyVISRSSKKKEDAIK-MGADHYI-ATLEEGDWGEKYFDTFD 245
Cdd:cd08267   147 vlingasgGVG--------------TFAVQIAKALGAH--VTGVCSTRNAELVRsLGADEVIdYTTEDFVALTAGGEKYD 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 246 LIVVCASSlTDIDFNIMPKAMKVGGRIVSISIPEQ-----HEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEKNIK 320
Cdd:cd08267   211 VIFDAVGN-SPFSLYRASLALKPGGRYVSVGGGPSglllvLLLLPLTLGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLK 289

                         330       340
                  ....*....|....*....|....*..
gi 2507698970 321 VWV-ETLPVGEAGvhEALERMERGDVR 346
Cdd:cd08267   290 PVIdSVYPLEDAP--EAYRRLKSGRAR 314
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-346 8.00e-15

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 74.23  E-value: 8.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGvgaqvfsclecdrck 107
Cdd:cd08271    23 PGP-GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKV-TGWKVGDRVA--------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 sdnepyctkfvttysqpYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVY-------------SPLVR 174
Cdd:cd08271    86 -----------------YHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYqalfkklrieagrTILIT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 175 NGCGpgkkvgivglgGIGSMGTLISKAMGAetYVISRSSKKKEDAIK-MGADHYIATLEEgDWGEKYFDT-----FDLIV 248
Cdd:cd08271   149 GGAG-----------GVGSFAVQLAKRAGL--RVITTCSKRNFEYVKsLGADHVIDYNDE-DVCERIKEItggrgVDAVL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 249 VCASSLTDIDfniMPKAMKVGGRIVsiSIPEQHEMLTLKPYGLkAVSISYSALGS---------IKELKQ----LLALVS 315
Cdd:cd08271   215 DTVGGETAAA---LAPTLAFNGHLV--CIQGRPDASPDPPFTR-ALSVHEVALGAahdhgdpaaWQDLRYageeLLELLA 288

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2507698970 316 EKNI-KVWVETLPVgEAGVhEALERMERGDVR 346
Cdd:cd08271   289 AGKLePLVIEVLPF-EQLP-EALRALKDRHTR 318
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 27-154 1.61e-14

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 74.11  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVfSCLECDRC 106
Cdd:cd08283    19 DPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGP-EVRNLKVGDRVVVPFTI-ACGECFYC 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507698970 107 KSDNEPYC------TKFVTTYSQP------YED---GYisQGGYANYVRV-HEHF-IVPIPENVP 154
Cdd:cd08283    97 KRGLYSQCdntnpsAEMAKLYGHAgagifgYSHltgGY--AGGQAEYVRVpFADVgPFKIPDDLS 159
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 34-343 3.22e-14

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 72.22  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAGHWGNMKMPLvvGHEIVGKVVRLGDKsNSGLKVGQRVgVGaqvfsclecdrcksdnepy 113
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALGLLPGDETPL--GLECSGIVTRVGSG-VTGLKVGDRV-MG------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 114 ctkfvttysqpyedgyISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVR-------------NGCGPg 180
Cdd:cd05195    58 ----------------LAPGAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDlarlqkgesvlihAAAGG- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 181 kkvgivglggigsMGTL---ISKAMGAETYVISRSSKKKEDAIKMG--ADH--------YIATLEEGDWGEKyfdtFDLI 247
Cdd:cd05195   121 -------------VGQAaiqLAQHLGAEVFATVGSEEKREFLRELGgpVDHifssrdlsFADGILRATGGRG----VDVV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 248 VvcaSSLTDIDFNIMPKAMKVGGRIVSIS--IPEQHEMLTLKPYglkAVSISYSA--LGSIKE---------LKQLLALV 314
Cdd:cd05195   184 L---NSLSGELLRASWRCLAPFGRFVEIGkrDILSNSKLGMRPF---LRNVSFSSvdLDQLARerpellrelLREVLELL 257

                         330       340
                  ....*....|....*....|....*....
gi 2507698970 315 SEKNIKVwVETLPVGEAGVHEALERMERG 343
Cdd:cd05195   258 EAGVLKP-LPPTVVPSASEIDAFRLMQSG 285
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-352 7.83e-14

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 71.48  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMK-MPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAQVFSclecdr 105
Cdd:cd08268    24 APGA---GEVLIRVEAIGLNRADAMFRRGAYIEPPpLPARLGYEAAGVVEAVGAGV-TGFAVGDRVSVIPAADL------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 cksdnepyctkfvTTYsqpyedgyisqGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGcGPGKKVGI 185
Cdd:cd08268    94 -------------GQY-----------GTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELA-GLRPGDSV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 186 VGLGGIGSMGTL---ISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFDT----FDLIV--VCASSLTD 256
Cdd:cd08268   149 LITAASSSVGLAaiqIANAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRITggkgVDVVFdpVGGPQFAK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 257 IdfnimPKAMKVGGRIVS--------ISIPEQ---HEMLTLKPYGLKAVSISYSALGSIKELkqLLALVSEKNIKVWV-E 324
Cdd:cd08268   229 L-----ADALAPGGTLVVygalsgepTPFPLKaalKKSLTFRGYSLDEITLDPEARRRAIAF--ILDGLASGALKPVVdR 301

                         330       340
                  ....*....|....*....|....*...
gi 2507698970 325 TLPVGEagVHEALERMERGDVRYRFTLI 352
Cdd:cd08268   302 VFPFDD--IVEAHRYLESGQQIGKIVVT 327
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 16-336 2.35e-13

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 70.40  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  16 EDWKNPkktkyDPKPfydHDVDIKIEACGVCGSDV-------------------HCAAGHWGN-MKMPLVVGHEIVGKVV 75
Cdd:cd08274    19 DDVPVP-----TPAP---GEVLIRVGACGVNNTDIntregwystevdgatdstgAGEAGWWGGtLSFPRIQGADIVGRVV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  76 RLGDKSNSGLkVGQRVgvgaQVFSCLecdRCKSDNEPYCTKFVttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPS 155
Cdd:cd08274    91 AVGEGVDTAR-IGERV----LVDPSI---RDPPEDDPADIDYI---------GSERDGGFAEYTVVPAENAYPVNSPLSD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 156 HLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTL-ISKAMGAetYVISRSSKKKEDAIK-MGADHYIATLEE 233
Cdd:cd08274   154 VELATFPCSYSTAENMLERAGVGAGETVLVTGASGGVGSALVqLAKRRGA--IVIAVAGAAKEEAVRaLGADTVILRDAP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 234 GDWGEKYFD--TFDLIV-VCASSLtdidFNIMPKAMKVGGRIVS---ISIPEQHemLTLKPYGLKAVSISYSALGSIKEL 307
Cdd:cd08274   232 LLADAKALGgePVDVVAdVVGGPL----FPDLLRLLRPGGRYVTagaIAGPVVE--LDLRTLYLKDLTLFGSTLGTREVF 305

                         330       340       350
                  ....*....|....*....|....*....|
gi 2507698970 308 KQLLALVSEKNIKVWVE-TLPVGEagVHEA 336
Cdd:cd08274   306 RRLVRYIEEGEIRPVVAkTFPLSE--IREA 333
PRK10083 PRK10083
putative oxidoreductase; Provisional
 35-159 7.62e-13

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 68.61  E-value: 7.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSNSGlKVGQRVGVGAqVFSCLECDRCKSDNEPYC 114
Cdd:PRK10083   26 EVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAA-RIGERVAVDP-VISCGHCYPCSIGKPNVC 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2507698970 115 TKFVTTysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAA 159
Cdd:PRK10083  104 TSLVVL-------GVHRDGGFSEYAVVPAKNAHRIPDAIADQYAV 141
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 27-345 2.75e-12

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 66.70  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMK-MPLVVGHEIVGKVVRLGDkSNSGLKVGQRVgvgaqvfsclecdr 105
Cdd:cd05276    22 KPAP-GPGEVLIRVAAAGVNRADLLQRQGLYPPPPgASDILGLEVAGVVVAVGP-GVTGWKVGDRV-------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 cksdnepyCtkfvttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLV-RNGCGPGKKvg 184
Cdd:cd05276    86 --------C-------------ALLAGGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFqLGGLKAGETvl 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 185 ivg-lggigSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEgDWGEKYFDTF-----DLIV--VCASSLTD 256
Cdd:cd05276   145 ihggasgvgTAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTE-DFAEEVKEATggrgvDVILdmVGGDYLAR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 257 idfNImpKAMKVGGRIVSISIpeqheM----------------LTLKPYGLKAVSISY-SALgsIKEL-KQLLALVSEKN 318
Cdd:cd05276   224 ---NL--RALAPDGRLVLIGL-----LggakaeldlapllrkrLTLTGSTLRSRSLEEkAAL--AAAFrEHVWPLFASGR 291

                         330       340
                  ....*....|....*....|....*...
gi 2507698970 319 IKVWV-ETLPVGEAGvhEALERMERGDV 345
Cdd:cd05276   292 IRPVIdKVFPLEEAA--EAHRRMESNEH 317
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 33-343 1.01e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 65.25  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACgvcgS----DVHCAAGHWGN-MKMPLVVGHEIVGKVVRLGDKsNSGLKVGQRVgvgaqvfsclecdrck 107
Cdd:cd08276    27 PGEVLVRVHAV----SlnyrDLLILNGRYPPpVKDPLIPLSDGAGEVVAVGEG-VTRFKVGDRV---------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 sdnepyctkfVTTYSQPYEDGYIS------------QGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRN 175
Cdd:cd08276    86 ----------VPTFFPNWLDGPPTaedeasalggpiDGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 176 G-CGPGKKVGIvglggigsMGT--------LISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWGEKYFD-T-- 243
Cdd:cd08276   156 GpLKPGDTVLV--------QGTggvslfalQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPDWGEEVLKlTgg 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 244 --FDLI--VVCASSLT-DIdfnimpKAMKVGGRIVSI-SIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLALVSEK 317
Cdd:cd08276   228 rgVDHVveVGGPGTLAqSI------KAVAPGGVISLIgFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAH 301

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2507698970 318 NIKvwvetlPV-------GEAgvHEALERMERG 343
Cdd:cd08276   302 RIR------PVidrvfpfEEA--KEAYRYLESG 326
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 28-345 1.44e-11

Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 64.77  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfydHDVDIKIEACGVCGSDVHCAAGHWgNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVgVGAQVFSCLECDRCK 107
Cdd:cd05279    23 PKA---GEVRIKVVATGVCHTDLHVIDGKL-PTPLPVILGHEGAGIVESIGP-GVTTLKPGDKV-IPLFGPQCGKCKQCL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 SDNEPYCTKF-VTTYSQPYEDG-------------YISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLV 173
Cdd:cd05279    97 NPRPNLCSKSrGTNGRGLMSDGtsrftckgkpihhFLGTSTFAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYGAAV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 174 RN-GCGPGKKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSKKKEDAIKMGADHYI-----------ATLEEGDWGEKY 240
Cdd:cd05279   177 NTaKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIaVDINKDKFEKAKQLGATECInprdqdkpiveVLTEMTDGGVDY 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 241 fdTFDlivvCASSLtdidfNIMPKAMKV----GGRIVSISIPEQHEMLTLKPYGL-KAVSISYSALGSIKELKQLLALVS 315
Cdd:cd05279   257 --AFE----VIGSA-----DTLKQALDAtrlgGGTSVVVGVPPSGTEATLDPNDLlTGRTIKGTVFGGWKSKDSVPKLVA 325

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2507698970 316 E---KNIKV---WVETLPVGEagVHEALERMERGDV 345
Cdd:cd05279   326 LyrqKKFPLdelITHVLPFEE--INDGFDLMRSGES 359
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 26-346 1.48e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 64.57  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  26 YDPKPFYDHDVD----------IKIEACGVCGSDVhcaAGHWGNMKMPLVVGHEIVGKVVRLGDKSnsglKVGQRVgVGA 95
Cdd:cd08242     7 DGGLDLRVEDLPkpepppgealVRVLLAGICNTDL---EIYKGYYPFPGVPGHEFVGIVEEGPEAE----LVGKRV-VGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  96 QVFSCLECDRCKSDNEPYCtkfvttysqPYED--GYISQ-GGYANYVRVHEHFIVPIPENVPSHLAA---PLLcgglTVY 169
Cdd:cd08242    79 INIACGRCEYCRRGLYTHC---------PNRTvlGIVDRdGAFAEYLTLPLENLHVVPDLVPDEQAVfaePLA----AAL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 170 SPLVRNGCGPGKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGadhyIATLEEGDWGEKYfDTFDLIVV 249
Cdd:cd08242   146 EILEQVPITPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLG----VETVLPDEAESEG-GGFDVVVE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 250 CASSLTdiDFNIMPKAMKVGGRIVSISIPEQHEMLTLKPYGLKAVSISYSALGSIKELKQLLAlvsekNIKVWVETL--- 326
Cdd:cd08242   221 ATGSPS--GLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGSRCGPFAPALRLLR-----KGLVDVDPLita 293

                         330       340
                  ....*....|....*....|...
gi 2507698970 327 --PVGEAgvHEALER-MERGDVR 346
Cdd:cd08242   294 vyPLEEA--LEAFERaAEPGALK 314
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 34-169 2.49e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 63.82  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAG-HWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGvgaqvfsCLecdrcksdnep 112
Cdd:cd08273    28 GEVVVKVEASGVSFADVQMRRGlYPDQPPLPFTPGYDLVGRVDALGSGV-TGFEVGDRVA-------AL----------- 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2507698970 113 yctkfvTTYsqpyedgyisqGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVY 169
Cdd:cd08273    89 ------TRV-----------GGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAY 128
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 27-141 4.39e-11

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 63.38  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGnMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAQVfSCLECDRC 106
Cdd:cd08282    19 DPKIEHPTDAIVRITTTAICGSDLHMYRGRTG-AEPGLVLGHEAMGEVEEVGS-AVESLKVGDRVVVPFNV-ACGRCRNC 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2507698970 107 KSDNEPYCTkfvTTYSQP------YEDGYISQGGYANYVRV 141
Cdd:cd08282    96 KRGLTGVCL---TVNPGRaggaygYVDMGPYGGGQAEYLRV 133
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 30-225 4.81e-11

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 63.26  E-value: 4.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  30 PFYDHDVDIKIEACGVCGSDVH------CAAghwGNMKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVGVGAQVfSCLEC 103
Cdd:PLN02702   38 PLGPHDVRVRMKAVGICGSDVHylktmrCAD---FVVKEPMVIGHECAGIIEEVGSEVKH-LVVGDRVALEPGI-SCWRC 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 104 DRCKSDNEPYC--TKFVTTysQPYedgyisQGGYANYVrVH-EHFIVPIPENVPSHLAAplLCGGLTV-YSPLVRNGCGP 179
Cdd:PLN02702  113 NLCKEGRYNLCpeMKFFAT--PPV------HGSLANQV-VHpADLCFKLPENVSLEEGA--MCEPLSVgVHACRRANIGP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2507698970 180 GKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSKKK-EDAIKMGAD 225
Cdd:PLN02702  182 ETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERlSVAKQLGAD 228
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 27-237 4.85e-11

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 63.10  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHwGNMKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVgVGAQVFSCLECdrc 106
Cdd:cd08287    19 DPVIEEPTDAVIRVVATCVCGSDLWPYRGV-SPTRAPAPIGHEFVGVVEEVGSEVTS-VKPGDFV-IAPFAISDGTC--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 ksdnePYCTKFVTTYSQPYED-GYISQGGYANYVRV--HEHFIVPIPEN-------VPSHLAAPLLCGglTVYSPLVRNG 176
Cdd:cd08287    93 -----PFCRAGFTTSCVHGGFwGAFVDGGQGEYVRVplADGTLVKVPGSpsddedlLPSLLALSDVMG--TGHHAAVSAG 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2507698970 177 CGPGKKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSKKKEDAIKMGADHYIAtlEEGDWG 237
Cdd:cd08287   166 VRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIaMSRHEDRQALAREFGATDIVA--ERGEEA 225
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 28-345 9.72e-11

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 62.28  E-value: 9.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfydHDVDIKIEACGVCGSDVHCAAGHWGNMK-MPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgvgaqvfsclecdrc 106
Cdd:TIGR02824  25 PKA---GEVLIRVAAAGVNRPDLLQRAGKYPPPPgASDILGLEVAGEVVAVGEGV-SRWKVGDRV--------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 ksdnepyCtkfvttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLV-RNGCGPGKKVGI 185
Cdd:TIGR02824  86 -------C-------------ALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFqRGGLKAGETVLI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 186 VGLGGIG-SMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEgDWGE--------KYFDTFdLIVVCASSLTD 256
Cdd:TIGR02824 146 HGGASGIgTTAIQLAKAFGARVFTTAGSDEKCAACEALGADIAINYREE-DFVEvvkaetggKGVDVI-LDIVGGSYLNR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 257 idfNImpKAMKVGGRIVSISI----PEQhemLTLKPYGLKAVSISYSALGS---------IKELKQ-LLALVSEKNIKVW 322
Cdd:TIGR02824 224 ---NI--KALALDGRIVQIGFqggrKAE---LDLGPLLAKRLTITGSTLRArpvaekaaiAAELREhVWPLLASGRVRPV 295

                         330       340
                  ....*....|....*....|....
gi 2507698970 323 V-ETLPVGEAGvhEALERMERGDV 345
Cdd:TIGR02824 296 IdKVFPLEDAA--QAHALMESGDH 317
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 28-228 5.69e-10

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 59.96  E-value: 5.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFYDH--DVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVGAqVFSCLECDR 105
Cdd:cd08286    18 PKPTIQEptDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGS-AVTNFKVGDRVLISC-ISSCGTCGY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 CKSDNEPYCTkfvttySQPYEDGYISQGGYANYVRV-HEHF-IVPIPENVPshLAAPLLCGGL--TVYSPLVRN------ 175
Cdd:cd08286    96 CRKGLYSHCE------SGGWILGNLIDGTQAEYVRIpHADNsLYKLPEGVD--EEAAVMLSDIlpTGYECGVLNgkvkpg 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507698970 176 ------GCGPgkkvgivglggiGSMGTLISKAM--GAETYVISRSSKKKEDAIKMGADHYI 228
Cdd:cd08286   168 dtvaivGAGP------------VGLAALLTAQLysPSKIIMVDLDDNRLEVAKKLGATHTV 216
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 35-154 8.30e-10

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 59.56  E-value: 8.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVGAqVFSCLECDRCKSDNEPYC 114
Cdd:cd08285    26 DAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEV-KDFKPGDRVIVPA-ITPDWRSVAAQRGYPSQS 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2507698970 115 tkfvTTYSQPYEDGYISQGGYANYVRVHEHF--IVPIPENVP 154
Cdd:cd08285   104 ----GGMLGGWKFSNFKDGVFAEYFHVNDADanLAPLPDGLT 141
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-343 1.16e-09

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 59.14  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFYDHdVDIKIEACGVCGSDVHCAAGHWGN-MKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGVgaqvfsclecdrc 106
Cdd:cd08275    22 PEPSSGE-VRVRVEACGLNFADLMARQGLYDSaPKPPFVPGFECAGTVEAVGE-GVKDFKVGDRVMG------------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 ksdnepyCTKFvttysqpyedgyisqGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVY-------------SPLV 173
Cdd:cd08275    87 -------LTRF---------------GGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYyalfelgnlrpgqSVLV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 174 RN---GCGpgkkvgivglggigSMGTLISKAMGAETyVISRSSKKKEDAIK-MGADHYIATLEEgDWGEK----YFDTFD 245
Cdd:cd08275   145 HSaagGVG--------------LAAGQLCKTVPNVT-VVGTASASKHEALKeNGVTHVIDYRTQ-DYVEEvkkiSPEGVD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 246 LIVVCassLTDIDFNIMPKAMKVGGRIVSISIpeqHEMLTLKPYGLKAVSISY----------------SALG------- 302
Cdd:cd08275   209 IVLDA---LGGEDTRKSYDLLKPMGRLVVYGA---ANLVTGEKRSWFKLAKKWwnrpkvdpmklisenkSVLGfnlgwlf 282

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2507698970 303 -----SIKELKQLLALVSEKNIKVWV-ETLPVGEagVHEALERMERG 343
Cdd:cd08275   283 eerelLTEVMDKLLKLYEEGKIKPKIdSVFPFEE--VGEAMRRLQSR 327
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 27-226 1.28e-09

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 58.52  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAA---GHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVgaqvfsclec 103
Cdd:cd08269    14 RPTP-GPGQVLVRVEGCGVCGSDLPAFNqgrPWFVYPAEPGGPGHEGWGRVVALGPGV-RGLAVGDRVAG---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 104 drcksdnepyctkfvttysqpyedgyISQGGYANYVRVHEHFIVPIPENVPSHL--AAPLLCG--GLTVYSPLvrngcgP 179
Cdd:cd08269    82 --------------------------LSGGAFAEYDLADADHAVPLPSLLDGQAfpGEPLGCAlnVFRRGWIR------A 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2507698970 180 GKKVGIVGLGGIGSMGTLISKAMGAETY-VISRSSKKKEDAIKMGADH 226
Cdd:cd08269   130 GKTVAVIGAGFIGLLFLQLAAAAGARRViAIDRRPARLALARELGATE 177
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 28-239 1.69e-09

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 58.22  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfydHDVDIKIEACGVCGSDVHCAAGHWgNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVGvgaqvfsclecdrck 107
Cdd:cd05286    24 PGP---GEVLVRNTAIGVNFIDTYFRSGLY-PLPLPFVLGVEGAGVVEAVGP-GVTGFKVGDRVA--------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 sdnepYCTKFvttysqpyedgyisqGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT-------VYSP------LVR 174
Cdd:cd05286    84 -----YAGPP---------------GAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTahyllreTYPVkpgdtvLVH 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 175 NGCGpGkkvgivglggigsMGTL---ISKAMGAEtyVISR-SSKKKED-AIKMGADHYIATLEEgDWGEK 239
Cdd:cd05286   144 AAAG-G-------------VGLLltqWAKALGAT--VIGTvSSEEKAElARAAGADHVINYRDE-DFVER 196
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 28-176 1.73e-09

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 58.48  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKpfyDHDVDIKIEACGVCGSDVHCAAGHWGnMKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVgVGAQVFSCLECDRCK 107
Cdd:cd08299    30 PK---AHEVRIKIVATGICRSDDHVVSGKLV-TPFPVILGHEAAGIVESVGEGVTT-VKPGDKV-IPLFVPQCGKCRACL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 SDNEPYCTKF-VTTYSQPYEDG-------------YISQGGYANYVRVHEHFIVPIPEnvpshlAAPLL------CGGLT 167
Cdd:cd08299   104 NPESNLCLKNdLGKPQGLMQDGtsrftckgkpihhFLGTSTFSEYTVVDEIAVAKIDA------AAPLEkvcligCGFST 177


                  ....*....
gi 2507698970 168 VYSPLVRNG 176
Cdd:cd08299   178 GYGAAVNTA 186
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 28-346 4.19e-09

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 57.21  E-value: 4.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFyDHDVDIKIEACGVCGSDVHCAAGHWGNmKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgvgaqvfsclecdrck 107
Cdd:cd08249    22 PKPG-PDEVLVKVKAVALNPVDWKHQDYGFIP-SYPAILGCDFAGTVVEVGSGV-TRFKVGDRV---------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 sdnepyctkfvTTYSQPYEDGYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVG 187
Cdd:cd08249    83 -----------AGFVHGGNPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGLPLPPPKPSP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 188 LGGIG---------SMGTL---ISKAMGAEtyVISRSSKKKEDAIK-MGADH---Y------IATLEEGDWGEKY-FDTF 244
Cdd:cd08249   152 ASKGKpvliwggssSVGTLaiqLAKLAGYK--VITTASPKNFDLVKsLGADAvfdYhdpdvvEDIRAATGGKLRYaLDCI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 245 ---DLIVVCASSLTDIDfnimpkamkvGGRIVSISiPEQHEmlTLKPYGLKAVSIS-YSALGSIKE-----------LKQ 309
Cdd:cd08249   230 stpESAQLCAEALGRSG----------GGKLVSLL-PVPEE--TEPRKGVKVKFVLgYTVFGEIPEdrefgevfwkyLPE 296

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2507698970 310 LLAlvsEKNIK-VWVETLPVGEAGVHEALERMERGDVR 346
Cdd:cd08249   297 LLE---EGKLKpHPVRVVEGGLEGVQEGLDLLRKGKVS 331
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 27-291 3.22e-08

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 54.53  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHdVDIKIEACGVCGSDVHCAAGHWGnmKMP-----LVVGHEIVGKVVRLGDksNSGLKVGQRVgVGAQVFSCL 101
Cdd:cd08230    20 EPEPTPGE-VLVRTLEVGVCGTDREIVAGEYG--TAPpgedfLVLGHEALGVVEEVGD--GSGLSPGDLV-VPTVRRPPG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 102 ECDRCKSDNEPYCTKfvTTYsqpYEDGYISQGGY-ANYVRVHEHFIVPIPENVPSH--LAAPLLCG------GLTVYSPL 172
Cdd:cd08230    94 KCLNCRIGRPDFCET--GEY---TERGIKGLHGFmREYFVDDPEYLVKVPPSLADVgvLLEPLSVVekaieqAEAVQKRL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 173 VRNGC------GPGkkvgivglggigSMGTLIS---KAMGAETYVISRSSK---KKEDAIKMGAdHYIATLEEGDWGEKY 240
Cdd:cd08230   169 PTWNPrralvlGAG------------PIGLLAAlllRLRGFEVYVLNRRDPpdpKADIVEELGA-TYVNSSKTPVAEVKL 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507698970 241 FDTFDLIVVC--ASSLTdidFNIMPkAMKVGGRIVSISIPEQHEMLTLKPYGL 291
Cdd:cd08230   236 VGEFDLIIEAtgVPPLA---FEALP-ALAPNGVVILFGVPGGGREFEVDGGEL 284
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 28-174 3.77e-08

Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 54.65  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfydHDVDIKIEACGVCGSDVHCAAGhWGNMKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVgVGAQVFSCLECDRCK 107
Cdd:cd08277    25 PKA---NEVRIKMLATSVCHTDILAIEG-FKATLFPVILGHEGAGIVESVGEGVTN-LKPGDKV-IPLFIGQCGECSNCR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 108 SDNEPYCTKFVTTYSQPYEDG-------------YISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVR 174
Cdd:cd08277    99 SGKTNLCQKYRANESGLMPDGtsrftckgkkiyhFLGTSTFSQYTVVDENYVAKIDPAAPLEHVCLLGCGFSTGYGAAWN 178
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 27-342 4.27e-08

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 54.13  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNM-KMPLVVGHEIVGKVVRLGDkSNSGLKVGQRV---GVGAQVfscle 102
Cdd:cd08253    22 VPTP-GPGEVLVRVHASGVNPVDTYIRAGAYPGLpPLPYVPGSDGAGVVEAVGE-GVDGLKVGDRVwltNLGWGR----- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 103 cdrcksdnepyctkfvttysqpyedgyiSQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCG-PGK 181
Cdd:cd08253    95 ----------------------------RQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAkAGE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 182 KVgivglggigsmgtLIS--------------KAMGAETYVISRSSKKKEDAIKMGADHYIATLEEgDWGEK-----YFD 242
Cdd:cd08253   147 TV-------------LVHggsgavghaavqlaRWAGARVIATASSAEGAELVRQAGADAVFNYRAE-DLADRilaatAGQ 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 243 TFDLIV-VCASSLTDIDFNImpkaMKVGGRIVSISIPEQHEMLTLKPYGLKAVSI--------SYSALGSIkeLKQLLAL 313
Cdd:cd08253   213 GVDVIIeVLANVNLAKDLDV----LAPGGRIVVYGSGGLRGTIPINPLMAKEASIrgvllytaTPEERAAA--AEAIAAG 286

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2507698970 314 VSEKNIKVWVE-TLPVGEAG-VHEALERMER 342
Cdd:cd08253   287 LADGALRPVIArEYPLEEAAaAHEAVESGGA 317
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 35-346 5.04e-08

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 53.72  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNM-KMPLVVGHEIVGKVVRLGDkSNSGLKVGQRV-----GVGAQvfsclecdrcks 108
Cdd:cd08272    29 QVLVRVHASGVNPLDTKIRRGGAAARpPLPAILGCDVAGVVEAVGE-GVTRFRVGDEVygcagGLGGL------------ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 109 dnepyctkfvttysqpyedgyisQGGYANYVRVHEHFIVPIPENVpSHL-AAPLLCGGLTVYSPLVRNG-CGPGKKVgiv 186
Cdd:cd08272    96 -----------------------QGSLAEYAVVDARLLALKPANL-SMReAAALPLVGITAWEGLVDRAaVQAGQTV--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 187 glggigsmgtLI--------------SKAMGAETYViSRSSKKKEDAIKMGADH----------YIATLEEGDWGEKYFD 242
Cdd:cd08272   149 ----------LIhggaggvghvavqlAKAAGARVYA-TASSEKAAFARSLGADPiiyyretvveYVAEHTGGRGFDVVFD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 243 TFDLIVVCASsltdidfnimPKAMKVGGRIVSISIPEQHEmltLKPYGLKAVSISY-------------SALGSIkeLKQ 309
Cdd:cd08272   218 TVGGETLDAS----------FEAVALYGRVVSILGGATHD---LAPLSFRNATYSGvftllplltgegrAHHGEI--LRE 282

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2507698970 310 LLALVSEKNIKVWVE--TLPVGEAGvhEALERMERGDVR 346
Cdd:cd08272   283 AARLVERGQLRPLLDprTFPLEEAA--AAHARLESGSAR 319
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 35-176 9.22e-08

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 53.15  E-value: 9.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  35 DVDIKIEACGVCGSDVHCAAGHWGNmKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVgVGAQVFSCLECDRCKSDNEPYC 114
Cdd:cd08281    35 EVLVKIAAAGLCHSDLSVINGDRPR-PLPMALGHEAAGVVVEVGEGVTD-LEVGDHV-VLVFVPSCGHCRPCAEGRPALC 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 115 TK-----------------FVTTYSQPYEDGyISqgGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLT-----VYSPL 172
Cdd:cd08281   112 EPgaaangagtllsggrrlRLRGGEINHHLG-VS--AFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLTgvgavVNTAG 188


                  ....
gi 2507698970 173 VRNG 176
Cdd:cd08281   189 VRPG 192
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 28-346 1.25e-07

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 52.61  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFYDHDVDIKIEACGVCGSDVHCAAGHwG----NMKM------------PLVVGHEIVGKVVRLGDKSNSgLKVGQRV 91
Cdd:cd08248    24 PVIRKPNQVLIKVHAASVNPIDVLMRSGY-GrtllNKKRkpqsckysgiefPLTLGRDCSGVVVDIGSGVKS-FEIGDEV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  92 GVGAQVFSclecdrcksdnepyctkfvttysqpyedgyisQGGYANYVRVHEHFIVPIPENVpSHL-AAPLLCGGLTVYS 170
Cdd:cd08248   102 WGAVPPWS--------------------------------QGTHAEYVVVPENEVSKKPKNL-SHEeAASLPYAGLTAWS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 171 PLVR-----------------NGCGPgkkvgivglggigsMGTLIS---KAMGAETYVISrSSKKKEDAIKMGADHYIAT 230
Cdd:cd08248   149 ALVNvgglnpknaagkrvlilGGSGG--------------VGTFAIqllKAWGAHVTTTC-STDAIPLVKSLGADDVIDY 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 231 LEEGDWGE-KYFDTFDLIVVCASSLTDIdfnIMPKAMKVGGRIVSISIPEQHEM-----------------LTLKPYGLK 292
Cdd:cd08248   214 NNEDFEEElTERGKFDVILDTVGGDTEK---WALKLLKKGGTYVTLVSPLLKNTdklglvggmlksavdllKKNVKSLLK 290

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2507698970 293 AVSISY---SALGSIkeLKQLLALVSEKNIKVWVE-TLPVGEagVHEALERMERGDVR 346
Cdd:cd08248   291 GSHYRWgffSPSGSA--LDELAKLVEDGKIKPVIDkVFPFEE--VPEAYEKVESGHAR 344
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 28-169 1.74e-07

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 52.26  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPfYDHDVDIKIEACGVCGSDV-HCAAGHWGNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVgvgaqvfsclecdrc 106
Cdd:cd08250    26 PLP-GPGEVLVKNRFVGINASDInFTAGRYDPGVKPPFDCGFEGVGEVVAVGE-GVTDFKVGDAV--------------- 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507698970 107 ksdnepyctkfvttysqpyedGYISQGGYANYVRVHEHFIVPIPENVPSHLaaPLLCGGLTVY 169
Cdd:cd08250    89 ---------------------ATMSFGAFAEYQVVPARHAVPVPELKPEVL--PLLVSGLTAS 128
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
28-232 2.87e-07

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 51.76  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFYDH--DVDIKIEACGVCGSDVHCAAGHwGNMKMPLVVGHEIVGKVVRLGdKSNSGLKVGQRVGVgAQVFSCLECDR 105
Cdd:PRK10309   18 PIPEIKHqdDVLVKVASSGLCGSDIPRIFKN-GAHYYPITLGHEFSGYVEAVG-SGVDDLHPGDAVAC-VPLLPCFTCPE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 106 CKSDNEPYCTKFVTTYSQpyedgyiSQGGYANYVRVHEHFIVPIPENVPSHLAA---PLLCGgltVYSPLVRNGCgPGKK 182
Cdd:PRK10309   95 CLRGFYSLCAKYDFIGSR-------RDGGNAEYIVVKRKNLFALPTDMPIEDGAfiePITVG---LHAFHLAQGC-EGKN 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2507698970 183 VGIVGLGGIGSMGTLISKAMGAETY-VISRSSKKKEDAIKMGADHYIATLE 232
Cdd:PRK10309  164 VIIIGAGTIGLLAIQCAVALGAKSVtAIDINSEKLALAKSLGAMQTFNSRE 214
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 38-343 3.16e-07

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 51.23  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970   38 IKIEACGVCGSDVHCAAGhwgNMKMPLVVGHEIVGKVVRLGDkSNSGLKVGQRVgVGaqvfsclecdrcksdnepyctkf 117
Cdd:smart00829   1 IEVRAAGLNFRDVLIALG---LYPGEAVLGGECAGVVTRVGP-GVTGLAVGDRV-MG----------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  118 vttysqpyedgyISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVY-------------SPLVRNGCGpgkkvg 184
Cdd:smart00829  53 ------------LAPGAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYyalvdlarlrpgeSVLIHAAAG------ 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  185 ivglggigsmGT-----LISKAMGAETYViSRSSKKKEDAIK-MG-ADHYI--------------ATLEEGdwgekyfdt 243
Cdd:smart00829 115 ----------GVgqaaiQLARHLGAEVFA-TAGSPEKRDFLRaLGiPDDHIfssrdlsfadeilrATGGRG--------- 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  244 FDLIVvcaSSLTDiDFniMPKAMKV---GGRIVSISI-----PEQHEMLTLKPyglkavSISYSA--LGSIKE------- 306
Cdd:smart00829 175 VDVVL---NSLSG-EF--LDASLRClapGGRFVEIGKrdirdNSQLAMAPFRP------NVSYHAvdLDALEEgpdrire 242

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2507698970  307 -LKQLLALVSEKNIK-VWVETLPVGEagVHEALERMERG 343
Cdd:smart00829 243 lLAEVLELFAEGVLRpLPVTVFPISD--AEDAFRYMQQG 279
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 28-272 4.66e-07

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 51.07  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  28 PKPFYDHdVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVrlgDKSNSGLKVGQRV-----GVGaqvfscle 102
Cdd:cd08243    23 PEPKPGW-VLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVE---EAPGGTFTPGQRVatamgGMG-------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 103 cdrcksdnepyctkfvTTYSqpyedgyisqGGYANYVRVHEHFIVPIPENVP-SHLAA-PLLcgGLTVYSPLVRN-GCGP 179
Cdd:cd08243    91 ----------------RTFD----------GSYAEYTLVPNEQVYAIDSDLSwAELAAlPET--YYTAWGSLFRSlGLQP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 180 GKKVGIVGLGGIGSMGTL-ISKAMGAETYVISRSSKKKEDAIKMGADHYIatLEEGDWGE---KYFDTFDLI--VVCASS 253
Cdd:cd08243   143 GDTLLIRGGTSSVGLAALkLAKALGATVTATTRSPERAALLKELGADEVV--IDDGAIAEqlrAAPGGFDKVleLVGTAT 220

                         250
                  ....*....|....*....
gi 2507698970 254 LTDidfniMPKAMKVGGRI 272
Cdd:cd08243   221 LKD-----SLRHLRPGGIV 234
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 63-239 8.50e-06

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 46.89  E-value: 8.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  63 PLVVGHEIVGKVVRLGDKSnSGLKVGQRVGVgaqvfsclecdrcksdnepyctkfvttysqpyedgYISQGGYANYVRVH 142
Cdd:cd05282    57 PAVPGNEGVGVVVEVGSGV-SGLLVGQRVLP-----------------------------------LGGEGTWQEYVVAP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 143 EHFIVPIPENVPSHLAAPLLCGGLTVY------------SPLVRNGCGP--GKkvgivglggigsMGTLISKAMGAETYV 208
Cdd:cd05282   101 ADDLIPVPDSISDEQAAMLYINPLTAWlmlteylklppgDWVIQNAANSavGR------------MLIQLAKLLGFKTIN 168

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2507698970 209 ISRSSKKKEDAIKMGADHyIATLEEGDWGEK 239
Cdd:cd05282   169 VVRRDEQVEELKALGADE-VIDSSPEDLAQR 198
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 34-247 2.96e-05

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 45.30  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVgVGAQVFSCLECDRCKSDNEPY 113
Cdd:cd08300    28 GEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTS-VKPGDHV-IPLYTPECGECKFCKSGKTNL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 114 CTKFVTTYSQ---PyeDG-------------YISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPlVRNGC 177
Cdd:cd08300   106 CQKIRATQGKglmP--DGtsrfsckgkpiyhFMGTSTFSEYTVVAEISVAKINPEAPLDKVCLLGCGVTTGYGA-VLNTA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 178 gpgkKVGIVGLGGIGSMGTL-ISKAMGA------ETYVISRSSKKKEDAIKMGADHYI-----------ATLEEGDWGEK 239
Cdd:cd08300   183 ----KVEPGSTVAVFGLGAVgLAVIQGAkaagasRIIGIDINPDKFELAKKFGATDCVnpkdhdkpiqqVLVEMTDGGVD 258


                  ....*...
gi 2507698970 240 YfdTFDLI 247
Cdd:cd08300   259 Y--TFECI 264
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 34-164 4.04e-05

Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 44.98  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  34 HDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSNsGLKVGQRVgvgAQVFS--CLECDRCKSDNE 111
Cdd:cd08301    28 MEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVT-DLKPGDHV---LPVFTgeCKECRHCKSEKS 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2507698970 112 PYCTKFVTTYSQ--PYEDG-------------YISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCG 164
Cdd:cd08301   104 NMCDLLRINTDRgvMINDGksrfsingkpiyhFVGTSTFSEYTVVHVGCVAKINPEAPLDKVCLLSCG 171
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 27-168 4.86e-05

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 44.52  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPFYDHDVDIKIEACGVCGSDVHCAAGHWGNMK-MPLVVGHEIVGKVVRLGDKSNSGLKVGQRVGVGAQvfsclecdr 105
Cdd:cd08291    24 EVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKaLPVPPGFEGSGTVVAAGGGPLAQSLIGKRVAFLAG--------- 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507698970 106 cksdnepyctkfvttysqpyedgyiSQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTV 168
Cdd:cd08291    95 -------------------------SYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTA 132
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 60-273 6.70e-05

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 44.18  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  60 MKMPLVVGHEIVGKVVRLGDKsNSGLKVGQRVGVGaqvfsclecdrcksdnepyctkfvttysqpyedgyisqGGYANYV 139
Cdd:cd08255    18 LPLPLPPGYSSVGRVVEVGSG-VTGFKPGDRVFCF--------------------------------------GPHAERV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 140 RVHEHFIVPIPENVPSHLAApLLCGGLTVYSPLVRNGCGPGKKVGivglggIGSMGTL------ISKAMGAET-YVISRS 212
Cdd:cd08255    59 VVPANLLVPLPDGLPPERAA-LTALAATALNGVRDAEPRLGERVA------VVGLGLVgllaaqLAKAAGAREvVGVDPD 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507698970 213 SKKKEDAIKMGADHYIATLEEGDWGEkyfDTFDLIVVCASSLTDIDFNImpKAMKVGGRIV 273
Cdd:cd08255   132 AARRELAEALGPADPVAADTADEIGG---RGADVVIEASGSPSALETAL--RLLRDRGRVV 187
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 33-233 1.09e-03

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 40.49  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACGVCGSDVHCAAGHWGNM-KMPLVVGHEIVGKVVRLGDKSNSgLKVGQRVGVGAQVfsclecdrcksdne 111
Cdd:cd08251     7 PGEVRIQVRAFSLNFGDLLCVRGLYPTMpPYPFTPGFEASGVVRAVGPHVTR-LAVGDEVIAGTGE-------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 112 pyctkfvttysqpyedgyiSQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGI 191
Cdd:cd08251    72 -------------------SMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTATGG 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2507698970 192 GS-MGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEE 233
Cdd:cd08251   133 TGlMAVQLARLKGAEIYATASSDDKLEYLKQLGVPHVINYVEE 175
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 27-343 2.47e-03

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 39.43  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  27 DPKPfYDHDVDIKIEACGVCGSDVHCAAGHWGNMKMPLVVGHEIVGKVVRLGDKSnSGLKVGQRVgvgaqvfsclecdrc 106
Cdd:cd08252    25 KPVP-GGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEV-TLFKVGDEV--------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 107 ksdnepyctkfvttysqpYEDGYIS-QGGYANYVRVHEHFIVPIPENVpSHLAA---PLLcgGLTVY------------- 169
Cdd:cd08252    88 ------------------YYAGDITrPGSNAEYQLVDERIVGHKPKSL-SFAEAaalPLT--SLTAWealfdrlgiseda 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 170 -----SPLVRNGCGpGkkvgivglggIGSMGTLISKAMGAETyVISRSSK--KKEDAIKMGADHYI----ATLEEGDWGE 238
Cdd:cd08252   147 enegkTLLIIGGAG-G----------VGSIAIQLAKQLTGLT-VIATASRpeSIAWVKELGADHVInhhqDLAEQLEALG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 239 kyFDTFDLIVvcasSLTDID--FNIMPKAMKVGGRIVSISipEQHEMLTLKPYGLKAVSI--------SYSALGSI---- 304
Cdd:cd08252   215 --IEPVDYIF----CLTDTDqhWDAMAELIAPQGHICLIV--DPQEPLDLGPLKSKSASFhwefmftrSMFQTPDMieqh 286

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2507698970 305 KELKQLLALVSEKNIKVWV-ETL-PVGEAGVHEALERMERG 343
Cdd:cd08252   287 EILNEVADLLDAGKLKTTLtETLgPINAENLREAHALLESG 327
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 33-237 4.08e-03

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 38.94  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  33 DHDVDIKIEACGVCGSDVHCAAGHwgnmkmPL----------------VVGHEIVGKVVRLGDKSNsGLKVGQRVgvgaq 96
Cdd:cd08246    42 PGEVLVAVMAAGVNYNNVWAALGE------PVstfaarqrrgrdepyhIGGSDASGIVWAVGEGVK-NWKVGDEV----- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970  97 VFSCLECDRcksdNEPYCTKFVTTYSQP-----YEDGYisqGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSP 171
Cdd:cd08246   110 VVHCSVWDG----NDPERAGGDPMFDPSqriwgYETNY---GSFAQFALVQATQLMPKPKHLSWEEAAAYMLVGATAYRM 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 172 LVR---NGCGPGKKVGI-VGLGGIGSMGTLISKAMGAETYVISRSSKKKEDAIKMGADHYIATLEEGDWG 237
Cdd:cd08246   183 LFGwnpNTVKPGDNVLIwGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGAEGVINRRDFDHWG 252
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 128-239 8.12e-03

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 37.70  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698970 128 GYISQGGYANYVRVHEHFIVPIPENVPSHLAAPLLCGGLTVYSPLVRNGCgpGKKVGIVGLGGIGS-MGTL---ISKAMG 203
Cdd:PTZ00354   88 ALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGD--VKKGQSVLIHAGASgVGTAaaqLAEKYG 165

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2507698970 204 AETyVISRSSKKKEDAIK-MGADHYIATLEEGDWGEK 239
Cdd:PTZ00354  166 AAT-IITTSSEEKVDFCKkLAAIILIRYPDEEGFAPK 201
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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